Structural stability of Calmodulin-target peptide complex at different temperatures based on molecular dynamics simulation.

ABSTRACT: Calmodulin (CaM) is a multifunctional protein commonly found in various eukaryotic cells that can bind Ca²⁺, making it highly valuable for research in agriculture, medicine, the environment, and other fields. Protein functionality is intricately linked to its structure. To understand how varying temperatures affect the structural integrity of CaM protein at the molecular level, the effect of temperature on the structural stability of CaM-peptide complex was investigated based on the molecular dynamics (MD) simulation. Some analyses including the root mean square deviation (RMSD) values, interaction energies, the decomposition of total energy of the system, the binding mechanism for Ca²⁺, and the secondary structure of CaM-peptide at different temperatures have been ma

SUBMITTER: Ding J 

PROVIDER: S-EPMC12102965 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature