Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure.

ABSTRACT: Application of hydrostatic pressure shifts protein conformational equilibria in a direction to reduce the volume of the system. A current view is that the volume reduction is dominated by elimination of voids or cavities in the protein interior via cavity hydration, although an alternative mechanism wherein cavities are filled with protein side chains resulting from a structure relaxation has been suggested [López CJ, Yang Z, Altenbach C, Hubbell WL (2013) Proc Natl Acad Sci USA 110(46):E4306-E4315]. In the present study, mechanisms for elimination of cavities under high pressure are investigated in the L99A cavity mutant of T4 lysozyme and derivatives thereof using site-directed spin labeling, pressure-resolved double electron-electron resonance, and high-pressure circular dichroism spect

SUBMITTER: Lerch MT 

PROVIDER: S-EPMC4434698 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature