Solvent effects in the slow dynamics of proteins

Abstract : The influence of solvent on the slow internal dynamics of proteins is studied by comparing Molecular Dynamics simulations of solvated and unsolvated lysozyme. The dynamical trajectories are projected onto the protein's normal modes in order to obtain a separate analysis for each of the associated time scales. The results show that solvent effects are important for the slowest motions (below 1ps−1) but negligible for faster motions. The damping effects seen in the latter show that the principal source of friction in protein dynamics is not the solvent, but the protein itself.
Keywords : friction normal modes
Document type :
Journal articles
Complete list of metadatas
Contributor : Isabelle Frapart <>
Submitted on : Wednesday, October 3, 2007 - 10:25:25 AM
Last modification on : Tuesday, June 18, 2019 - 11:46:04 AM

Links full text



Konrad Hinsen, Gérald Kneller. Solvent effects in the slow dynamics of proteins. Proteins - Structure, Function and Bioinformatics, Wiley, 2008, 70 (4), pp.1235-1242. ⟨10.1002/prot.21655⟩. ⟨hal-00176279⟩



Record views