Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.

ABSTRACT: Proteins are inherently plastic molecules, whose function often critically depends on excursions between different molecular conformations (conformers). However, a rigorous understanding of the relation between a protein's structure, dynamics and function remains elusive. This is because many of the conformers on its energy landscape are only transiently formed and marginally populated (less than a few per cent of the total number of molecules), so that they cannot be individually characterized by most biophysical tools. Here we study a lysozyme mutant from phage T4 that binds hydrophobic molecules and populates an excited state transiently (about 1 ms) to about 3% at 25 °C (ref. 5). We show that such binding occurs only via the ground state, and present the atomic-level model of the 'invi

SUBMITTER: Bouvignies G 

PROVIDER: S-EPMC3706084 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature