TNNC1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TNNI2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin.
1. The p.m.r. spectra of the larger CNBr-cleavage peptides of troponin I from rabbit fast-twitch skeletal muscle corresponded largely to those of fairly flexible solution structures. 2. On addition of troponin C to each of the CNBr-cleavage peptides in turn, perturbations of side chains were noted only for peptides CN5 (residues 1-21) and CN4 (residues 96-116). 3. In the presence ... [more]
Throughput
- Low Throughput
Additional Notes
- pmr spectra
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| TNNI2 TNNC1 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 0.9997 | BioGRID | 3193030 |
Curated By
- BioGRID