Conformational Dynamics Govern the Free-Energy Landscape of a Membrane-Interacting Protein.

ABSTRACT: The equilibrium stabilities and the folding rates of membrane-bound proteins are determined by hydrophobic and polar intermolecular contacts with their environment as well as by intramolecular packing and conformational dynamics. The contributions of these factors, however, remain elusive and might vary considerably among proteins. Mistic from Bacillus subtilis is a particularly intriguing example of an α-helical protein that associates with membranes in spite of its unusual hydrophilicity. In micelles, Mistic is stabilized by hydrophobic and polar interactions with detergents, but it is unclear whether and how these intermolecular contacts are coupled to structural and dynamic adaptations of the protein itself. Here, we investigated the packing and the conformational dynamics of Mi

SUBMITTER: Frotscher E 

PROVIDER: S-EPMC6690567 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature