FB-IS-009In Silico2026-06-25
All-Atom Conformational Ensemble of MOTS-c against Mitochondrial Complexes I and IV under Simulated HEV Stress
Abstract
An in-silico structural modeling study predicting the docking topology and dynamic interface of the mitochondrial-derived peptide MOTS-c against active subunits of Mitochondrial Complexes I and IV. Electrostatic persistence and relative free energies of binding were calculated across conformer ensembles.
Methods
- 01Models : Complex I and IV cryo-EM structural models
- 02Peptide structure : MOTS-c primary sequence, fully folded conformers
- 03Docking method : flexible interface docking with all-atom representation
- 04Analysis : electrostatic salt-bridges and interface hydrogen bonding
DISCLOSURE : This report presents anonymized in-silico and/or observational reference data. It does not establish a causal relationship between any catalogued material and any physiological outcome, and it is not a claim of safety, efficacy, or benefit.
Relevant Reference Materials
This report's structural and literature findings are studied against the following catalogued reference material.