Titin
UniProt Q8WZ42 · gene TTN · Homo sapiens · 34350 residues
279evidence items
19mapped to a state
2states
8techniques
6sources
0conflicts
Coverage grid
Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).
| State | Basis | xray | cryoem | nmr_structure | nmr_shifts | saxs_sans | cd | force_spectroscopy | md | Total |
|---|---|---|---|---|---|---|---|---|---|---|
| folded Ig domain I27-folded | observed | proc 3 | proc 1 | proc 3 | · | · | · | · | · | 7 |
| unfolded under force I27-unfolded | inferred (one method) | · | · | · | · | · | · | rep 12 | · | 12 |
Unmapped evidence: 260 of 279 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| BMRB | 2 | 0 |
| DisProt | 1 | 0 |
| MDDB | 2 | 0 |
| RCSB PDB | 66 | 7 |
| SASBDB | 8 | 0 |
| SMASH-BIO | 200 | 12 |
Curated rules applied
i27-force-unfolded: 12 itemsi27-structures-folded: 6 items
Structure
Choose a state. Each model is badged observed or inferred; assumptions are one click away.
States and transitions
| State | Basis | Parent | Description |
|---|---|---|---|
| folded Ig domain I27-folded | observed | — | Folded Ig repeat 27 in solution, as in 1TIT (NMR, minimised average structure). |
| unfolded under force I27-unfolded | inferred | — | Unfolded state reached under mechanical load. No observed structure.Assumptions (3)
|
No transitions recorded in this version (no rate or free-energy evidence has been curated yet).
Evidence
One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-1BPV-1 RCSB PDB | nmr_structure | structure | in vitro · 36.85 °C · pH 5.6 TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES · TITIN (chains A) | unmapped |
| EV-PDB-1G1C-1 RCSB PDB | xray | resolution: 2.1 Å | in vitro · -173.15 °C · pH 8 I1 DOMAIN FROM TITIN · IMMUNOGLOBULIN-LIKE DOMAIN I1 FROM TITIN (chains A,B) | unmapped |
| EV-PDB-1NCT-1 RCSB PDB | nmr_structure | structure | in vitro · 26.85 °C · pH 4.8 TITIN MODULE M5, N-TERMINALLY EXTENDED, NMR · TITIN (chains A) | unmapped |
| EV-PDB-1NCU-1 RCSB PDB | nmr_structure | structure | in vitro · 26.85 °C · pH 4.8 Titin Module M5, N-terminally Extended, NMR · TITIN (chains A) | unmapped |
| EV-PDB-1TIT-1 RCSB PDB | nmr_structure | structure | in vitro TITIN, IG REPEAT 27, NMR, MINIMIZED AVERAGE STRUCTURE · TITIN, I27 (chains A) | folded Ig domain · curator:draft (unreviewed) · high NMR structure of folded Ig repeat 27; representative for the folded state. |
| EV-PDB-1TIU-1 RCSB PDB | nmr_structure | structure | in vitro TITIN, IG REPEAT 27, NMR, 24 STRUCTURES · TITIN, I27 (chains A) | folded Ig domain · rule:i27-structures-folded · medium Structure titled as I27 (I91); other titin domains are excluded by title. |
| EV-PDB-1TNN-1 RCSB PDB | nmr_structure | structure | in vitro Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I set · TITIN MODULE M5 (chains A) | unmapped |
| EV-PDB-1WAA-3 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · ligands ZN IG27 protein domain · TITIN (chains F) | folded Ig domain · rule:i27-structures-folded · medium Structure titled as I27 (I91); other titin domains are excluded by title. |
| EV-PDB-1WAA-2 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · ligands ZN IG27 protein domain · TITIN (chains E) | folded Ig domain · rule:i27-structures-folded · medium Structure titled as I27 (I91); other titin domains are excluded by title. |
| EV-PDB-1WAA-1 RCSB PDB | xray | resolution: 1.8 Å | in vitro · -173.15 °C · ligands ZN IG27 protein domain · TITIN (chains A,B,C,D) | folded Ig domain · rule:i27-structures-folded · medium Structure titled as I27 (I91); other titin domains are excluded by title. |
| EV-PDB-1YA5-1 RCSB PDB | xray | resolution: 2.445 Å | in vitro · -173.15 °C · pH 4.45 · ligands SO4 Crystal structure of the titin domains z1z2 in complex with telethonin · N2B-TITIN ISOFORM (chains A,B) | unmapped |
| EV-PDB-2A38-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 5.5 · ligands CD Crystal structure of the N-Terminus of titin · Titin (chains A,B,C) | unmapped |
| EV-PDB-2BK8-1 RCSB PDB | xray | resolution: 1.69 Å | in vitro · -173.15 °C · pH 7 M1 domain from titin · TITIN HEART ISOFORM N2-B (chains A) | unmapped |
| EV-PDB-2F8V-1 RCSB PDB | xray | resolution: 2.75 Å | in vitro · -173.15 °C · pH 4.45 · ligands SO4 Structure of full length telethonin in complex with the N-terminus of titin · N2B-Titin Isoform (chains A,B,C,D) | unmapped |
| EV-PDB-2ILL-1 RCSB PDB | xray | resolution: 2.2 Å | in vitro · -173.15 °C · ligands CL Anomalous substructure of Titin-A168169 · Titin (chains A) | unmapped |
| EV-PDB-2J8H-1 RCSB PDB | xray | resolution: 1.99 Å | in vitro · -173.15 °C · pH 9 · ligands GOL Structure of the immunoglobulin tandem repeat A168-A169 of titin · TITIN (chains A) | unmapped |
| EV-PDB-2J8O-1 RCSB PDB | xray | resolution: 2.49 Å | in vitro · -173.15 °C · pH 9 · ligands GOL Structure of the immunoglobulin tandem repeat of titin A168-A169 · TITIN (chains A,B) | unmapped |
| EV-PDB-2NZI-1 RCSB PDB | xray | resolution: 2.9 Å | in vitro · -173.15 °C · pH 5.5 Crystal structure of domains A168-A170 from titin · Titin (chains A,B) | unmapped |
| EV-PDB-2WP3-2 RCSB PDB | xray | resolution: 1.48 Å | in vitro · -173.15 °C · pH 7 · ligands GOL, SO4 Crystal structure of the Titin M10-Obscurin like 1 Ig complex · TITIN (chains T) | unmapped |
| EV-PDB-2WWK-2 RCSB PDB | xray | resolution: 1.7 Å | in vitro · -173.15 °C · pH 5.5 · ligands GOL, SO4 Crystal structure of the Titin M10-Obscurin like 1 Ig F17R mutant complex · TITIN (chains T) | unmapped |
| EV-PDB-2WWM-2 RCSB PDB | xray | resolution: 2.3 Å | in vitro · -173.15 °C · pH 5 Crystal structure of the Titin M10-Obscurin like 1 Ig complex in space group P1 · TITIN (chains D,T) | unmapped |
| EV-PDB-2Y9R-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C · pH 6.5 · ligands 12P Crystal structure of the M10 domain of Titin · TITIN (chains T) | unmapped |
| EV-PDB-3B43-1 RCSB PDB | xray | resolution: 3.3 Å | in vitro · -173.15 °C · pH 4.9 I-band fragment I65-I70 from titin · Titin (chains A) | unmapped |
| EV-PDB-3KNB-1 RCSB PDB | xray | resolution: 1.4 Å | in vitro · -173.15 °C · pH 8 · ligands SO4 Crystal structure of the titin C-terminus in complex with obscurin-like 1 · Titin (chains A) | unmapped |
| EV-PDB-3LPW-1 RCSB PDB | xray | resolution: 1.65 Å | in vitro · -173.15 °C · ligands MPD, MRD Crystal structure of the FnIII-tandem A77-A78 from the A-band of titin · A77-A78 domain from Titin (chains A,B) | unmapped |
| EV-PDB-3PUC-1 RCSB PDB | xray | resolution: 0.96 Å | in vitro · -173.15 °C · pH 8 · ligands SO4 Atomic resolution structure of titin domain M7 · Titin (chains A) | unmapped |
| EV-PDB-3Q5O-1 RCSB PDB | xray | resolution: 2.05 Å | in vitro · -173.15 °C · pH 6.8 · ligands SO4 Crystal structure of human titin domain M10 · Titin (chains A,B) | unmapped |
| EV-PDB-3QP3-1 RCSB PDB | xray | resolution: 1.997 Å | in vitro · -173.15 °C · pH 4 · ligands SO4 Crystal structure of titin domain M4, tetragonal form · Titin (chains A,B,C) | unmapped |
| EV-PDB-4C4K-2 RCSB PDB | xray | resolution: 1.95 Å | in vitro · -173.15 °C · pH 8.5 · ligands EDO Crystal structure of the titin M10-Obscurin Ig domain 1 complex · TITIN (chains T) | unmapped |
| EV-PDB-4O00-1 RCSB PDB | xray | resolution: 1.853 Å | in vitro · -173.15 °C · pH 4 Crystal structure of the Titin A-band domain A3 · Titin (chains A,B) | unmapped |
| EV-PDB-4QEG-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 7.5 · ligands CA Crystal structure of domain I10 from titin (space group P41) · Titin (chains A) | unmapped |
| EV-PDB-4UOW-2 RCSB PDB | xray | resolution: 3.3 Å | in vitro · -173.15 °C · pH 3.6 · ligands CL, NA Crystal structure of the titin M10-Obscurin Ig domain 1 complex · Obscurin (chains 1,3,5,7,9,B,D,F,H,J,L,N,P,R,T,V,X,Z) | unmapped |
| EV-PDB-5BS0-3 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · pH 7 · ligands GOL, SO4 MAGE-A3 Reactive TCR in complex with Titin Epitope in HLA-A1 · Titin (chains C) | unmapped |
| EV-PDB-5JDD-1 RCSB PDB | xray | resolution: 1.53 Å | in vitro · -173.15 °C Crystal structure of I9-I11 tandem from titin (P212121) · Titin (chains A) | unmapped |
| EV-PDB-5JDE-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C Crystal structure of I9-I11 tandem from titin (P1) · Titin (chains A,B) | unmapped |
| EV-PDB-5JDJ-1 RCSB PDB | xray | resolution: 1.738 Å | in vitro · -173.15 °C · ligands CA Crystal structure of domain I10 from titin in space group P212121 · Titin (chains A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P) | unmapped |
| EV-PDB-5JOE-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C · pH 8.5 · ligands EDO, IPA Crystal structure of I81 from titin · Titin (chains A) | unmapped |
| EV-PDB-6FWX-1 RCSB PDB | xray | resolution: 3 Å | in vitro · -173.15 °C · ligands EDO Chimeric titin Z1Z2-Z1Z2 tandem (Z1212) functionalized with a GRGDS exogenous peptide from fibronectin · Titin,Titin,Titin (chains A,B) | unmapped |
| EV-PDB-6H4L-1 RCSB PDB | xray | resolution: 1.6 Å | in vitro · -173.15 °C · pH 6.5 · ligands CL, ZN Structure of Titin M4 trigonal form · Titin (chains A) | unmapped |
| EV-PDB-6HCI-1 RCSB PDB | xray | resolution: 2.12 Å | in vitro · -173.15 °C · pH 8 · ligands SO4 Crystal structure of titin M3 domain · Titin (chains A,B,C,D) | unmapped |
| EV-PDB-6I0Y-36 RCSB PDB | cryoem | resolution: 3.2 Å | in vitro · ligands MG, TRP, ZN TnaC-stalled ribosome complex with the titin I27 domain folding close to the ribosomal exit tunnel · Titin (chains z) | folded Ig domain · rule:i27-structures-folded · medium Structure titled as I27 (I91); other titin domains are excluded by title. |
| EV-PDB-6SDB-1 RCSB PDB | xray | resolution: 2.8 Å | in vitro · -173.15 °C · ligands ACT, EDO, PO4, SO4 Chimeric titin Z1Z2 functionalized with a KLER exogenous peptide from decorin · Titin,Decorin,Titin (chains A,B,C,D,E) | unmapped |
| EV-PDB-6YGN-1 RCSB PDB | xray | resolution: 2.4 Å | in vitro · -173.15 °C · ligands EDO, GOL Titin kinase and its flanking domains · Titin (chains A,B) | unmapped |
| EV-PDB-7AHS-1 RCSB PDB | xray | resolution: 2.05 Å | in vitro · -193.15 °C · ligands EDO, GOL, SO4 titin-N2A Ig81-Ig83 · Isoform 5 of Titin (chains A,B,C,D) | unmapped |
| EV-PDB-7NIP-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7.5 titin N2A unique sequence (UN2A) core · Isoform 11 of Titin (chains A) | unmapped |
| EV-PDB-8BNQ-1 RCSB PDB | xray | resolution: 2.3 Å | in vitro · 20 °C · ligands EDO Crystal structure of the FnIII-tandem A84-A86 from the A-band of titin · Titin (chains A,B) | unmapped |
| EV-PDB-6DL4-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7.5 Human Titin ZIg10 · Titin (chains A) | unmapped |
| EV-PDB-4JNW-1 RCSB PDB | xray | resolution: 2.06 Å | in vitro · -173.15 °C · ligands GOL Bacterially expressed Titin Kinase · Titin (chains A,B) | unmapped |
| EV-PDB-3LCY-1 RCSB PDB | xray | resolution: 2.5 Å | in vitro · -173.15 °C · pH 7.5 Titin Ig tandem domains A164-A165 · Titin (chains A,B,C,D) | unmapped |
| EV-PDB-2RQ8-1 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 7.4 Solution NMR structure of titin I27 domain mutant · Titin (chains A) | folded Ig domain · rule:i27-structures-folded · medium Structure titled as I27 (I91); other titin domains are excluded by title. |
| EV-PDB-1TNM-1 RCSB PDB | nmr_structure | structure | in vitro TERTIARY STRUCTURE OF AN IMMUNOGLOBULIN-LIKE DOMAIN FROM THE GIANT MUSCLE PROTEIN TITIN: A NEW MEMBER OF THE I SET · TITIN MODULE M5 (chains A) | unmapped |
| EV-PDB-1TKI-1 RCSB PDB | xray | resolution: 2 Å | in vitro · -173.15 °C AUTOINHIBITED SERINE KINASE DOMAIN OF THE GIANT MUSCLE PROTEIN TITIN · TITIN (chains A,B) | unmapped |
| EV-PDB-8G4L-4 RCSB PDB | cryoem | resolution: 6.4 Å | in vitro Cryo-EM structure of the human cardiac myosin filament · Titin (chains am,an,bm,bn,m,n) | unmapped |
| EV-PDB-8OQ9-1 RCSB PDB | xray | resolution: 1.65 Å | in vitro · -173.15 °C · ligands CL, ZN Crystal structure of the titin domain Fn3-56 · Titin (chains A,B,C) | unmapped |
| EV-PDB-8ORL-1 RCSB PDB | xray | resolution: 1.43 Å | in vitro · -173.15 °C · ligands CL, ZN Crystal structure of the S23226G missense variant of titin domain Fn3-56 · Titin (chains A,B,C) | unmapped |
| EV-PDB-8P35-1 RCSB PDB | xray | resolution: 2.2 Å | in vitro · -173.15 °C · pH 7.5 Mutant human titin immunoglobulin-like 21 domain - C3575S · Titin (chains A,B,C,D,E,F) | unmapped |
| EV-PDB-8OVU-1 RCSB PDB | xray | resolution: 1.95 Å | in vitro · -173.15 °C · pH 7.5 · ligands MG Human titin immunoglobulin-like 21 domain · Titin (chains A,B) | unmapped |
| EV-PDB-8OTY-1 RCSB PDB | xray | resolution: 1.9 Å | in vitro · -173.15 °C Crystal structure of the titin domain Fn3-90 · Titin (chains A,B,C,D) | unmapped |
| EV-PDB-8OT5-1 RCSB PDB | xray | resolution: 1.56 Å | in vitro · -173.15 °C · ligands CL, NA Crystal structure of the titin domain Fn3-85 · Titin (chains A,B,C,D,E,F) | unmapped |
| EV-PDB-8OSD-1 RCSB PDB | xray | resolution: 1.7 Å | in vitro · -173.15 °C Crystal structure of the titin domain Fn3-49 · Titin (chains A,B) | unmapped |
| EV-PDB-8OS3-1 RCSB PDB | xray | resolution: 1.68 Å | in vitro · -173.15 °C Crystal structure of the titin domain Fn3-11 · Titin (chains A) | unmapped |
| EV-PDB-8OMW-1 RCSB PDB | xray | resolution: 1.05 Å | in vitro · -173.15 °C · ligands CL Crystal structure of the titin domain Fn3-20 · Titin (chains A) | unmapped |
| EV-PDB-8OIY-1 RCSB PDB | xray | resolution: 2.1 Å | in vitro · -173.15 °C Crystal structure of the R15908H missense variant of titin domain Fn3-3 · Titin (chains A,B,C,D,E,F) | unmapped |
| EV-PDB-8BXR-1 RCSB PDB | xray | resolution: 2.7 Å | in vitro · -193.15 °C · ligands EDO Titin FnIII-domain I109-I111 (I/A4-A/A6) from the MIR region · Titin (chains A) | unmapped |
| EV-PDB-8BW6-1 RCSB PDB | xray | resolution: 1.95 Å | in vitro · -173.15 °C · ligands CA, EDO, PEG Titin FnIII-domain I110 (I/A6) from the MIR region · Titin (chains A) | unmapped |
| EV-PDB-8BVO-1 RCSB PDB | xray | resolution: 2.55 Å | in vitro · -193.15 °C Titin I110-I111 FnIII tandem from the MIR region (I/A5-I/A6) · Titin (chains A) | unmapped |
| EV-BMRB-30471 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 7.5 Human Titin ZIg10 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-50117 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 7.5 UN2A · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-SASBDB-SASDKA2 SASBDB | saxs_sans | radius_of_gyration: 2.976 nm ± 0.218 | in vitro · 10 °C · pH 7.6 Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins. · Two titin I27 domains linked with RS linker | unmapped |
| EV-SASBDB-SASDKB2 SASBDB | saxs_sans | radius_of_gyration: 2.976 nm ± 0.218 | in vitro · 10 °C · pH 7.6 Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins. · Two titin I27 domains linked with RS linker | unmapped |
| EV-SASBDB-SASDKC2 SASBDB | saxs_sans | radius_of_gyration: 2.94 nm ± 0.17 | in vitro · 10 °C · pH 7.6 Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins. · Two titin I27 domains linked with GGG linker | unmapped |
| EV-SASBDB-SASDKD2 SASBDB | saxs_sans | radius_of_gyration: 3.106 nm ± 0.156 | in vitro · 10 °C · pH 7.6 Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins. · Two titin I27 domains linked with VKA linker | unmapped |
| EV-SASBDB-SASDKE2 SASBDB | saxs_sans | radius_of_gyration: 3.09 nm ± 0.772 | in vitro · 10 °C · pH 7.6 Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins. · Two titin I27 domains linked with AAE linker | unmapped |
| EV-SASBDB-SASDMN9 SASBDB | saxs_sans | radius_of_gyration: 2.49 nm ± 0.007 | in vitro · pH 7.2 The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin · Titin | unmapped |
| EV-SASBDB-SASDMP9 SASBDB | saxs_sans | radius_of_gyration: 3.69 nm ± 0.016 | in vitro · pH 7.2 The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin · Titin | unmapped |
| EV-SASBDB-SASDMQ9 SASBDB | saxs_sans | radius_of_gyration: 3.69 nm ± 0.012 | in vitro · pH 7.2 The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin · Titin | unmapped |
| EV-DISPROT-DP00072r004 DisProt | cd | disorder_region: 26 residues | in vitro DisProt DP00072: disorder, residues 11045-11070 · residues 11045-11070; evidence: far-UV circular dichroism evidence used in manual assertion | unmapped |
| EV-MDDB-A00QK MDDB | md | trajectory: 10 ns | in silico · 26.85 °C MoDEL 1NCT · start 1NCT; Amber Parm99 | unmapped |
| EV-MDDB-A012C MDDB | md | trajectory: 10 ns | in silico · 26.85 °C MoDEL 1TIT · start 1TIT; Amber Parm99 | unmapped |
| EV-SMASH-SMFS-000147 SMASH-BIO | force_spectroscopy | study_record | in vitro Interdomain linkers tune the energy dissipation of immunoglobulin domains in titin. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000188 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanobiology of the diabetic cardiomyocyte: insulin signaling, titin elasticity, and multiscale mechanical dysfunction. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion, rheology_cell, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-000257 SMASH-BIO | force_spectroscopy | study_record | in vitro Resolving Heterogeneous Mechanical Domains via Physics-Aware Deep Clustering of Single-Molecule Force Spectroscopy Data · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000258 SMASH-BIO | force_spectroscopy | study_record | in vitro Resolving Orsay Virus δ Protein Architecture Using Molecular Rulers in Single-Molecule Force Spectroscopy · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000475 SMASH-BIO | force_spectroscopy | study_record | in vitro Intermolecular Misfolding Captured in Parallelly Organized Titin. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000508-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 5 pN | in vitro · pH 7.5 Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000645 SMASH-BIO | force_spectroscopy | study_record | in vitro Titin as a mechanical damper: Balancing Stability and longevity through inter-domain linker design · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-000658 SMASH-BIO | force_spectroscopy | study_record | in vitro Viscoelasticity of a single poly-protein probed step-by-step during its mechanical unfolding and refolding under the force-clamp conditions. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-000853 SMASH-BIO | force_spectroscopy | study_record | in vitro Modeling thick filament activation suggests a molecular basis for force depression. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-000954 SMASH-BIO | force_spectroscopy | study_record | in cell Split Luciferase Molecular Tension Sensors for Bioluminescent Readout of Mechanical Forces in Biological Systems. · Titin (Ig/FnIII domains, e.g. I27/I91); tension sensors; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-000961 SMASH-BIO | force_spectroscopy | study_record | in vitro Structural domain in the Titin N2B-us region binds to FHL2 in a force-activation dependent manner. · 6His-Avi-2I27-N2B-us-2I27-Spy (titin N2B unique sequence construct) (N2B-us (572 aa); structural domain IPEEQRLN…GAKT; truncation/deletion variants also tested); Titin I27 domains (2 on each side, mechanical fingerprint/spacers); magnetic tweezers; experiment class: unfolding_protein, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001138 SMASH-BIO | force_spectroscopy | study_record | in vitro Emulating Titin by a Multidomain DNA Structure. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001241 SMASH-BIO | force_spectroscopy | study_record | in vitro Modeling Thick Filament Activation Suggests a Molecular Basis for Force Depression · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-001319 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule analysis of osmolyte-mediated nanomechanical unfolding behavior of a protein domain. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001358 SMASH-BIO | force_spectroscopy | study_record | in vitro Theory of sarcomere assembly inferred from sequential ordering of myofibril components · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001364 SMASH-BIO | force_spectroscopy | study_record | in vitro Two-Molecule Force Spectroscopy on Proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001558 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001581 SMASH-BIO | force_spectroscopy | study_record | in vitro Measuring biological materials mechanics with atomic force microscopy - Mechanical unfolding of biopolymers. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-001586 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical Unfolding and Refolding of NanoLuc via Single-Molecule Force Spectroscopy and Computer Simulations. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001588-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 5 pN | in vitro Mechanical regulation of Titin N2B-us conformation and its binding to FHL2 · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001598 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanochemical Evolution of Disulfide Bonds in Proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001914 SMASH-BIO | force_spectroscopy | study_record | in vitro Enzymatic Protein-Protein Conjugation through Internal Site Verified at the Single-Molecule Level. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-001973 SMASH-BIO | force_spectroscopy | study_record | in vitro Interaction of chloramphenicol with titin I27 probed using single-molecule force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-001974 SMASH-BIO | force_spectroscopy | study_record | in vitro Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002083 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Protein Unfolding: Denaturant vs. Force. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002130-r1 SMASH-BIO | force_spectroscopy | unfolding_force: 10 pN | in vitro · pH 7.2 Single-Molecule Force Spectroscopy Studies of Missense Titin Mutations That Are Likely Causing Cardiomyopathy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002240 SMASH-BIO | force_spectroscopy | study_record | in vitro An Exactly Solvable Stochastic Kinetic Theory of Single-Molecule Force Experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002280 SMASH-BIO | force_spectroscopy | study_record | in vitro Contracting striated muscle has a dynamic I-band spring with an undamped stiffness 100 times larger than the passive stiffness. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-002286 SMASH-BIO | force_spectroscopy | study_record | in vitro Correlations within polyprotein forced unfolding dwell-times introduce sequential dependency. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002339 SMASH-BIO | force_spectroscopy | study_record | in vitro Exploiting a Mechanical Perturbation of a Titin Domain to Identify How Force Field Parameterization Affects Protein Refolding Pathways. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002417 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8 Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002438 SMASH-BIO | force_spectroscopy | study_record | in vitro Modulating mechanical stability of heterodimerization between engineered orthogonal helical domains. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002506 SMASH-BIO | force_spectroscopy | study_record | in vitro Rate-dependent force-extension models for single-molecule force spectroscopy experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002527-r0 SMASH-BIO | force_spectroscopy | persistence_length: 0.35 nm | in vitro · pH 7.2 Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002527-r1 SMASH-BIO | force_spectroscopy | contour_length: 39 nm | in vitro · pH 7.2 Single-Molecule Force Spectroscopy on the N2A Element of Titin: Effects of Phosphorylation and CARP. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002547 SMASH-BIO | force_spectroscopy | study_record | in vitro Stretching single titin molecules from failing human hearts reveals titin's role in blunting cardiac kinetic reserve. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-002594 SMASH-BIO | force_spectroscopy | study_record | in vitro Verification of sortase for protein conjugation by single-molecule force spectroscopy and molecular dynamics simulations. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002716 SMASH-BIO | force_spectroscopy | study_record | in vitro Exploiting a Mechanical Perturbation of Titin Domain to Identify How Force Field Parameterization Affects Protein Refolding Pathways · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-002879 SMASH-BIO | force_spectroscopy | study_record | in vitro Role of Diffusion in Unfolding and Translocation of Multidomain Titin I27 Substrates by a Clp ATPase Nanomachine. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: force_generation_motor, unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-002931 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 The Mechanical Power of Titin Folding. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-002966 SMASH-BIO | force_spectroscopy | study_record | in vitro Unveiling the influence of device stiffness in single macromolecule unfolding. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-003016 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Calcium increases titin N2A binding to F-actin and regulated thin filaments. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-003056 SMASH-BIO | force_spectroscopy | study_record | in vitro Deciphering the Mechanical Properties of Type III Secretion System EspA Protein by Single Molecule Force Spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003125 SMASH-BIO | force_spectroscopy | study_record | in vitro High-Speed Force Spectroscopy for Single Protein Unfolding. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003181-r0 SMASH-BIO | force_spectroscopy | folding_free_energy: 10 kBT | in vitro Mechanical responses of the mechanosensitive unstructured domains in cardiac titin. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003196 SMASH-BIO | force_spectroscopy | study_record | in vitro Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-003197 SMASH-BIO | force_spectroscopy | study_record | in vitro Monitoring Unfolding of Titin I27 single- and bi-Domain with High-Pressure NMR Spectroscopy · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-003271 SMASH-BIO | force_spectroscopy | study_record | in vitro Segmentation and the Entropic Elasticity of Modular Proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003303 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule force-unfolding of titin I27 reveals a correlation between the size of the surrounding anions and its mechanical stability. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-003332 SMASH-BIO | force_spectroscopy | study_record | in vitro The Mechanical Power of Protein Folding · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003337 SMASH-BIO | force_spectroscopy | study_record | in vitro The Work of Titin Protein Folding as a Major Driver in Muscle Contraction. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003351 SMASH-BIO | force_spectroscopy | study_record | in vitro Thick-Filament Extensibility in Intact Skeletal Muscle. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-003361 SMASH-BIO | force_spectroscopy | study_record | in vitro Two-State Folding Energy Determination Based on Transition Points in Nonequilibrium Single-Molecule Experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: nucleic_acid_mechanics, unfolding_nucleic_acid, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003416 SMASH-BIO | force_spectroscopy | study_record | in vitro Asymmetric Conformational Transitions in AAA+ Biological Nanomachines Modulate Direction-Dependent Substrate Protein Unfolding Mechanisms. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003424 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.5 Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003485 SMASH-BIO | force_spectroscopy | study_record | in vitro Elasticity of the Transition State Leading to an Unexpected Mechanical Stabilization of Titin Immunoglobulin Domains. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003515 SMASH-BIO | force_spectroscopy | study_record | in vitro Force generation by titin folding. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003549 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8 Increasing evidence of mechanical force as a functional regulator in smooth muscle myosin light chain kinase. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-003557 SMASH-BIO | force_spectroscopy | study_record | in vitro Introduction of steered molecular dynamics into UNRES coarse-grained simulations package. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003586 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003589 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanotransduction properties of the cytoplasmic tail of PECAM-1. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003600 SMASH-BIO | force_spectroscopy | study_record | in vitro Molecular stretching modulates mechanosensing pathways. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003604 SMASH-BIO | force_spectroscopy | study_record | in vitro Multidomain proteins under force. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003759 SMASH-BIO | force_spectroscopy | study_record | in vitro The influence of disulfide bonds on the mechanical stability of proteins is context dependent. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003795 SMASH-BIO | force_spectroscopy | study_record | in vitro α-Actinin/titin interaction: A dynamic and mechanically stable cluster of bonds in the muscle Z-disk. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-003834 SMASH-BIO | force_spectroscopy | study_record | in vitro Can Dissipative Properties of Single Molecules Be Extracted from a Force Spectroscopy Experiment? · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-003906 SMASH-BIO | force_spectroscopy | study_record | in vitro Force-dependent switch in protein unfolding pathways and transition-state movements. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-003938 SMASH-BIO | force_spectroscopy | study_record | in vitro Kinetic Ductility and Force-Spike Resistance of Proteins from Single-Molecule Force Spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003975 SMASH-BIO | force_spectroscopy | study_record | in vitro Monovalent Strep-Tactin for strong and site-specific tethering in nanospectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-003986 SMASH-BIO | force_spectroscopy | study_record | in vitro Nanopuller-open data acquisition platform for AFM force spectroscopy experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-004016 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004080 SMASH-BIO | force_spectroscopy | study_record | in vitro The Y9P Variant of the Titin I27 Module: Structural Determinants of Its Revisited Nanomechanics. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, translation_transcription_replication, unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-004090 SMASH-BIO | force_spectroscopy | study_record | in cell Titin-Based Nanoparticle Tension Sensors Map High-Magnitude Integrin Forces within Focal Adhesions. · Titin (Ig/FnIII domains, e.g. I27/I91); tension sensors; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004190 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces. · Titin (Ig/FnIII domains, e.g. I27/I91); magnetic tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004322 SMASH-BIO | force_spectroscopy | study_record | in vitro Optimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004326 SMASH-BIO | force_spectroscopy | study_record | in vitro Phosphorylating Titin's Cardiac N2B Element by ERK2 or CaMKIIδ Lowers the Single Molecule and Cardiac Muscle Force. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: membrane_mechanics, rheology_cell, translation_transcription_replication | unmapped |
| EV-SMASH-SMFS-004349 SMASH-BIO | force_spectroscopy | study_record | in vitro Rapid and Robust Polyprotein Production Facilitates Single-Molecule Mechanical Characterization of β-Barrel Assembly Machinery Polypeptide Transport Associated Domains. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004420 SMASH-BIO | force_spectroscopy | study_record | in vitro Titin domains progressively unfolded by force are homogenously distributed along the molecule. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004476 SMASH-BIO | force_spectroscopy | study_record | in vitro COARSE-GRAINED MODELING OF PROTEIN UNFOLDING DYNAMICS. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004477-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 90 pN | in vitro · pH 7.5 Ca2+ binding enhanced mechanical stability of an archaeal crystallin. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004477-r1 SMASH-BIO | force_spectroscopy | unfolding_force: 35 pN | in vitro · pH 7.5 Ca2+ binding enhanced mechanical stability of an archaeal crystallin. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004527 SMASH-BIO | force_spectroscopy | study_record | in vitro Discrimination among protein variants using an unfoldase-coupled nanopore. · Titin (Ig/FnIII domains, e.g. I27/I91); nanopore force; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004571 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Individual globular domains and domain unfolding visualized in overstretched titin molecules with atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004596 SMASH-BIO | force_spectroscopy | study_record | in vitro Low-force transitions in single titin molecules reflect a memory of contractile history. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004695 SMASH-BIO | force_spectroscopy | study_record | in vitro Single molecule mechanical manipulation for studying biological properties of proteins, DNA, and sugars. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: nucleic_acid_mechanics, receptor_ligand_adhesion, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004738 SMASH-BIO | force_spectroscopy | study_record | in vitro The structure of misfolded amyloidogenic dimers: computational analysis of force spectroscopy data. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004751 SMASH-BIO | force_spectroscopy | study_record | in vitro UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004818 SMASH-BIO | force_spectroscopy | study_record | in vitro Conformational plasticity of the essential membrane-associated mannosyltransferase PimA from mycobacteria. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-004881 SMASH-BIO | force_spectroscopy | study_record | in vitro High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004931 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanics of proteins with a focus on atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-004959-r0 SMASH-BIO | force_spectroscopy | rupture_force: 2000 pN | in vitro · pH 7.2 Nanomechanics of HaloTag tethers. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005023 SMASH-BIO | force_spectroscopy | study_record | in vitro Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005142 SMASH-BIO | force_spectroscopy | study_record | in vitro Computational investigation of the effect of thermal perturbation on the mechanical unfolding of titin I27. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-005352 SMASH-BIO | force_spectroscopy | study_record | in vitro Spontaneous dimerization of titin protein Z1Z2 domains induces strong nanomechanical anchoring. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005379 SMASH-BIO | force_spectroscopy | study_record | in vitro Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005391 SMASH-BIO | force_spectroscopy | study_record | in vitro Unraveling solvent-mediated reaction pathways leading to regiospecific mechanochemical cleavage of disulfide bonds in peptides. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005404 SMASH-BIO | force_spectroscopy | study_record | in vitro Worm-like Ising model for protein mechanical unfolding under the effect of osmolytes. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005406 SMASH-BIO | force_spectroscopy | study_record | in vitro A conditional gating mechanism assures the integrity of the molecular force-sensor titin kinase. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005462 SMASH-BIO | force_spectroscopy | study_record | in vitro Contrasting the individual reactive pathways in protein unfolding and disulfide bond reduction observed within a single protein. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005466 SMASH-BIO | force_spectroscopy | study_record | in vitro Cytoskeletal protein kinases: titin and its relations in mechanosensing. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005530 SMASH-BIO | force_spectroscopy | study_record | in vitro Improved resolution of tertiary structure elasticity in muscle protein. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005533-r0 SMASH-BIO | force_spectroscopy | rupture_force: 3.8 nN | in vitro Influence of external force on properties and reactivity of disulfide bonds. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-005612 SMASH-BIO | force_spectroscopy | study_record | in vitro Probing osmolyte participation in the unfolding transition state of a protein. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005699 SMASH-BIO | force_spectroscopy | study_record | in vitro β-Connectin studies by small-angle x-ray scattering and single-molecule force spectroscopy by atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005714 SMASH-BIO | force_spectroscopy | study_record | in vitro An improved strategy for generating forces in steered molecular dynamics: the mechanical unfolding of titin, e2lip3 and ubiquitin. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005718 SMASH-BIO | force_spectroscopy | study_record | in vitro Application of HaloTag protein to covalent immobilization of recombinant proteins for single molecule force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005742 SMASH-BIO | force_spectroscopy | study_record | in vitro Collapse dynamics of single proteins extended by force. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005811 SMASH-BIO | force_spectroscopy | study_record | in vitro How sequence determines elasticity of disordered proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-005824 SMASH-BIO | force_spectroscopy | study_record | in vitro Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005940 SMASH-BIO | force_spectroscopy | study_record | in vitro Tertiary and secondary structure elasticity of a six-Ig titin chain. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005946 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7 The effects of PKCalpha phosphorylation on the extensibility of titin's PEVK element. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-005956 SMASH-BIO | force_spectroscopy | study_record | in vitro Theory of Biopolymer Stretching at High Forces. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: nucleic_acid_mechanics | unmapped |
| EV-SMASH-SMFS-006106 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006122 SMASH-BIO | force_spectroscopy | study_record | in vitro Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-006141-r0 SMASH-BIO | force_spectroscopy | persistence_length: 1.2 nm | in vitro PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell | unmapped |
| EV-SMASH-SMFS-006157 SMASH-BIO | force_spectroscopy | study_record | in vitro Protein kinase G modulates human myocardial passive stiffness by phosphorylation of the titin springs. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: membrane_mechanics, rheology_cell | unmapped |
| EV-SMASH-SMFS-006179 SMASH-BIO | force_spectroscopy | study_record | in vitro Single homopolypeptide chains collapse into mechanically rigid conformations. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006184-r0 SMASH-BIO | force_spectroscopy | persistence_length: 0.2 nm | in vitro Single molecule force spectroscopy of the cardiac titin N2B element: effects of the molecular chaperone alphaB-crystallin with disease-causing mutations. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006211 SMASH-BIO | force_spectroscopy | study_record | in vitro Stretching and unfolding of multidomain biopolymers: a statistical mechanics theory of titin. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: nucleic_acid_mechanics, unfolding_nucleic_acid, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006223 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Temperature and chemical denaturant dependence of forced unfolding of titin I27. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-006250 SMASH-BIO | force_spectroscopy | study_record | in vitro Velocity convergence of free energy surfaces from single-molecule measurements using Jarzynski's equality. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006258 SMASH-BIO | force_spectroscopy | study_record | in vitro A new atomic force microscope force ramp technique using digital force feedback control reveals mechanically weak protein unfolding events. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006259 SMASH-BIO | force_spectroscopy | study_record | in vitro A single-molecule perspective on the role of solvent hydrogen bonds in protein folding and chemical reactions. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006266 SMASH-BIO | force_spectroscopy | study_record | in vitro An experimentally guided umbrella sampling protocol for biomolecules. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006283 SMASH-BIO | force_spectroscopy | study_record | in vitro Comparing proteins by their unfolding pattern. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006381 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanoenzymatics of titin kinase. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006385 SMASH-BIO | force_spectroscopy | study_record | in vitro Model for stretching and unfolding the giant multidomain muscle protein using single-molecule force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: nucleic_acid_mechanics, unfolding_nucleic_acid, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006401 SMASH-BIO | force_spectroscopy | study_record | in vitro New force replica exchange method and protein folding pathways probed by force-clamp technique. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006402 SMASH-BIO | force_spectroscopy | study_record | in vitro New method for deciphering free energy landscape of three-state proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006418 SMASH-BIO | force_spectroscopy | study_record | in vitro Predicting the order in which contacts are broken during single molecule protein stretching experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006428 SMASH-BIO | force_spectroscopy | study_record | in vitro Pulling single molecules of titin by AFM--recent advances and physiological implications. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006432-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 20 pN | in vitro Recombination of protein fragments: a promising approach toward engineering proteins with novel nanomechanical properties. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006436 SMASH-BIO | force_spectroscopy | study_record | in vitro Response to Bianco et al.: Interaction forces between F-actin and titin PEVK domain measured with optical tweezers. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: force_generation_motor | unmapped |
| EV-SMASH-SMFS-006457 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006466 SMASH-BIO | force_spectroscopy | study_record | in vitro Solvent molecules bridge the mechanical unfolding transition state of a protein. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006487 SMASH-BIO | force_spectroscopy | study_record | in vitro The effect of temperature on mechanical resistance of the native and intermediate states of I27. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-006543 SMASH-BIO | force_spectroscopy | study_record | in vitro Contour length and refolding rate of a small protein controlled by engineered disulfide bonds. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006580 SMASH-BIO | force_spectroscopy | study_record | in vitro Experimental free energy surface reconstruction from single-molecule force spectroscopy using Jarzynski's equality. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006594 SMASH-BIO | force_spectroscopy | study_record | in vitro Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-006615 SMASH-BIO | force_spectroscopy | study_record | in vitro Interaction forces between F-actin and titin PEVK domain measured with optical tweezers. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-006622 SMASH-BIO | force_spectroscopy | study_record | in vitro Ising-like model for protein mechanical unfolding. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006679 SMASH-BIO | force_spectroscopy | study_record | in vitro Quasi-simultaneous imaging/pulling analysis of single polyprotein molecules by atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006692 SMASH-BIO | force_spectroscopy | study_record | in vitro Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006716 SMASH-BIO | force_spectroscopy | study_record | in vitro Tandem repeating modular proteins avoid aggregation in single molecule force spectroscopy experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-006818 SMASH-BIO | force_spectroscopy | study_record | in vitro Frequency modulation atomic force microscopy reveals individual intermediates associated with each unfolded I27 titin domain. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-006842-r0 SMASH-BIO | force_spectroscopy | contour_length: 120 nm | in vitro Mechanical properties of cardiac titin's N2B-region by single-molecule atomic force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006920 SMASH-BIO | force_spectroscopy | study_record | in vitro The molecular elasticity of the insect flight muscle proteins projectin and kettin. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006931 SMASH-BIO | force_spectroscopy | study_record | in vitro Viscoelastic study of the mechanical unfolding of a protein by AFM. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006953 SMASH-BIO | force_spectroscopy | study_record | in vitro Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: force_generation_motor, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-006957 SMASH-BIO | force_spectroscopy | study_record | in vitro Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: nucleic_acid_protein_interaction, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007014 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007015 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical unfolding of ubiquitin molecules. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007027-r0 SMASH-BIO | force_spectroscopy | persistence_length: 0.3 nm | in vitro Myomesin is a molecular spring with adaptable elasticity. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007070 SMASH-BIO | force_spectroscopy | study_record | in vitro Stretching globular polymers. I. Single chains. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-007072 SMASH-BIO | force_spectroscopy | study_record | in vitro Study of the mechanical properties of myomesin proteins using dynamic force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007084-r0 SMASH-BIO | force_spectroscopy | persistence_length: 0.3 nm ± 0.04 | in vitro Titin PEVK segment: charge-driven elasticity of the open and flexible polyampholyte. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-007084-r1 SMASH-BIO | force_spectroscopy | persistence_length: 0.18 nm ± 0.03 | in vitro Titin PEVK segment: charge-driven elasticity of the open and flexible polyampholyte. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-007164 SMASH-BIO | force_spectroscopy | study_record | in vitro Multiple sources of passive stress relaxation in muscle fibres. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007209 SMASH-BIO | force_spectroscopy | study_record | in vitro Synthesis and single-molecule studies of a well-defined biomimetic modular multidomain polymer using a peptidomimetic beta-sheet module. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007212-r0 SMASH-BIO | force_spectroscopy | persistence_length: 2.9 nm | in vitro The elasticity of single titin molecules using a two-bead optical tweezers assay. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-007262 SMASH-BIO | force_spectroscopy | study_record | in vitro Hidden complexity in the mechanical properties of titin. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007269 SMASH-BIO | force_spectroscopy | study_record | in vitro Kinetics from nonequilibrium single-molecule pulling experiments. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007274 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical design of the first proximal Ig domain of human cardiac titin revealed by single molecule force spectroscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007276 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007278-r0 SMASH-BIO | force_spectroscopy | persistence_length: 1.5 nm | in vitro Mechanics and structure of titin oligomers explored with atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007327 SMASH-BIO | force_spectroscopy | study_record | in vitro A simple method for probing the mechanical unfolding pathway of proteins in detail. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007333 SMASH-BIO | force_spectroscopy | study_record | in vitro Cardiac titin: molecular basis of elasticity and cellular contribution to elastic and viscous stiffness components in myocardium. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007353 SMASH-BIO | force_spectroscopy | study_record | in vitro Force spectroscopy of single biomolecules. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007369 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007375 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Model peptide studies of sequence regions in the elastomeric biomineralization protein, Lustrin A. I. The C-domain consensus-PG-, -NVNCT-motif. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007376-r0 SMASH-BIO | force_spectroscopy | persistence_length: 0.65 nm | in vitro Molecular mechanics of cardiac titin's PEVK and N2B spring elements. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: membrane_mechanics, rheology_cell | unmapped |
| EV-SMASH-SMFS-007381 SMASH-BIO | force_spectroscopy | study_record | in vitro PEVK domain of titin: an entropic spring with actin-binding properties. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: force_generation_motor, rheology_cell | unmapped |
| EV-SMASH-SMFS-007393 SMASH-BIO | force_spectroscopy | study_record | in vitro Steered molecular dynamics studies of titin I1 domain unfolding. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: nucleic_acid_protein_interaction, receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007399 SMASH-BIO | force_spectroscopy | study_record | in vitro The effect of core destabilization on the mechanical resistance of I27. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unfolded under force · rule:i27-force-unfolded · low SMASH-BIO force record whose publication title names I27 or I91; force unfolding reaches the unfolded state. Most values are extracted automatically. |
| EV-SMASH-SMFS-007408 SMASH-BIO | force_spectroscopy | study_record | in vitro Unfolding of titin domains studied by molecular dynamics simulations. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007419 SMASH-BIO | force_spectroscopy | study_record | in vitro Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007437 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical fatigue in repetitively stretched single molecules of titin. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007440 SMASH-BIO | force_spectroscopy | study_record | in vitro Modeling AFM-induced PEVK extension and the reversible unfolding of Ig/FNIII domains in single and multiple titin molecules. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007449 SMASH-BIO | force_spectroscopy | study_record | in vitro Single molecule measurements of titin elasticity. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007452 SMASH-BIO | force_spectroscopy | study_record | in vitro Stepwise unfolding of titin under force-clamp atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007474 SMASH-BIO | force_spectroscopy | study_record | in vitro Computer modeling of force-induced titin domain unfolding. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007493 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical manipulation of single titin molecules with laser tweezers. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007500 SMASH-BIO | force_spectroscopy | study_record | in vitro Native topology determines force-induced unfolding pathways in globular proteins. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007523 SMASH-BIO | force_spectroscopy | study_record | in vitro Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007529 SMASH-BIO | force_spectroscopy | study_record | in vitro Titin elasticity in the context of the sarcomere: force and extensibility measurements on single myofibrils. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007532 SMASH-BIO | force_spectroscopy | study_record | in vitro Unfolding forces of titin and fibronectin domains directly measured by AFM. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007534 SMASH-BIO | force_spectroscopy | study_record | in vitro Unfolding proteins by external forces and temperature: the importance of topology and energetics. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007538 SMASH-BIO | force_spectroscopy | study_record | in vitro A kinetic molecular model of the reversible unfolding and refolding of titin under force extension. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007550 SMASH-BIO | force_spectroscopy | study_record | in vitro Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007559 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical unfolding intermediates in titin modules. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007569 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-molecule biomechanics with optical methods. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: force_generation_motor, translation_transcription_replication, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007574 SMASH-BIO | force_spectroscopy | study_record | in vitro Stretching single-domain proteins: phase diagram and kinetics of force-induced unfolding. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007590 SMASH-BIO | force_spectroscopy | study_record | in vitro Characterizing titin's I-band Ig domain region as an entropic spring. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: membrane_mechanics, receptor_ligand_adhesion, rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007592 SMASH-BIO | force_spectroscopy | study_record | in vitro Complete unfolding of the titin molecule under external force. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007612 SMASH-BIO | force_spectroscopy | study_record | in vitro Nature of PEVK-titin elasticity in skeletal muscle. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-007618-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 300 pN | in vitro The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. · Titin (Ig/FnIII domains, e.g. I27/I91); afm smfs; experiment class: unfolding_protein | unmapped |
| EV-SMASH-SMFS-007619 SMASH-BIO | force_spectroscopy | study_record | in vitro The molecular elasticity of the extracellular matrix protein tenascin. · Titin (Ig/FnIII domains, e.g. I27/I91); force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007624 SMASH-BIO | force_spectroscopy | study_record | in vitro Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: rheology_cell, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007633 SMASH-BIO | force_spectroscopy | study_record | in vitro Elasticity and unfolding of single molecules of the giant muscle protein titin. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: nucleic_acid_protein_interaction, unfolding_protein | unmapped |
| EV-SMASH-SMFS-007634 SMASH-BIO | force_spectroscopy | study_record | in vitro Folding-unfolding transitions in single titin molecules characterized with laser tweezers. · Titin (Ig/FnIII domains, e.g. I27/I91); optical tweezers; experiment class: membrane_mechanics, unfolding_protein | unmapped |
Conflicts
No conflicts found among comparable evidence.
271 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.
Downloads
- Protein bundle (JSON)
- I27-folded-cif (mmCIF, observed)
- I27-folded-pdb (PDB, observed)
- Curation file (YAML)