In Silico Analysis of Temperature-Induced Structural, Stability, and Flexibility Modulations in Camel Cytochrome c.

ABSTRACT: Cytochrome c is a critical protein in energy metabolism, and its structural adaptations to different temperatures play a key role in enabling species like the wild Bactrian camel (Camelus ferus) and the Arabian camel (Camelus dromedarius) to thrive in their respective cold and hot environments. This study investigates the structural, thermodynamic, and dynamic properties of cytochrome c at different temperatures. Thermal Titration Molecular Dynamics (TTMD) simulations, which involve analyzing protein behaviour across a range of temperatures, were carried out using GROMACS, with each simulation running for 100 nanoseconds, at 245 K, 280 K, 303 K, 308 K, and 320 K, to evaluate stability and flexibility. Structural alterations were indicated by an increase in root

SUBMITTER: Alkhatabi HA 

PROVIDER: S-EPMC11815751 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature