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.
Compounds referenced
This note surveys published work on the following compound. They are research materials, not treatments, and nothing here indicates they are suitable for any use in humans.