Ontology highlight
ABSTRACT:
SUBMITTER: Katava M
PROVIDER: S-EPMC5584445 | biostudies-literature | 2017 Aug
REPOSITORIES: biostudies-literature
Katava Marina M Stirnemann Guillaume G Zanatta Marco M Capaccioli Simone S Pachetti Maria M Ngai K L KL Sterpone Fabio F Paciaroni Alessandro A
Proceedings of the National Academy of Sciences of the United States of America 20170814 35
Internal subnanosecond timescale motions are key for the function of proteins, and are coupled to the surrounding solvent environment. These fast fluctuations guide protein conformational changes, yet their role for protein stability, and for unfolding, remains elusive. Here, in analogy with the Lindemann criterion for the melting of solids, we demonstrate a common scaling of structural fluctuations of lysozyme protein embedded in different environments as the thermal unfolding transition is app ...[more]