Conformational changes below the Tm: molecular dynamics studies of the thermal pretransition of ribonuclease A.

ABSTRACT: Recent work suggests that some native conformations of proteins can vary with temperature. To obtain an atomic-level description of this structural and conformational variation, we have performed all-atom, explicit-solvent molecular dynamics simulations of bovine pancreatic ribonuclease A (RNase A) up to its melting temperature (Tm approximately 337 K). RNase A has a thermal pretransition near 320 K [Stelea, S. D., Pancoska, P., Benight, A. S., and Keiderling, T. A. (2001) Protein Sci. 10, 970-978]. Our simulations identify a conformational change that coincides with this pretransition. Between 310 and 320 K, there is a small but significant decrease in the number of native contacts, beta-sheet hydrogen bonding, and deviation of backbone conformation from the starting structure, and an inc

SUBMITTER: Merkley ED 

PROVIDER: S-EPMC2532537 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature