An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H.

ABSTRACT: Dynamic processes are inherent properties of proteins and are crucial for a wide range of biological functions. To address how changes in protein sequence and structure affect dynamic processes, a quantitative comparison of microsecond-to-microsecond time scale conformational changes, measured by solution NMR spectroscopy, within homologous mesophilic and thermophilic ribonuclease H (RNase H) enzymes is presented. Kinetic transitions between the observed major state (high population) and alternate (low population) conformational state(s) of the substrate-binding handle region in RNase H from the mesophile Escherichia coli (ecRNH) and thermophile Thermus thermophilus (ttRNH) occur with similar kinetic exchange rate constants, but the difference in stability between exchanging conformers is

SUBMITTER: Butterwick JA 

PROVIDER: S-EPMC2242442 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature