Local Bilayer Hydrophobicity Modulates Membrane Protein Stability.

ABSTRACT: Through the insertion of nonpolar side chains into the bilayer, the hydrophobic effect has long been accepted as a driving force for membrane protein folding. However, how the changing chemical composition of the bilayer affects the magnitude of the side-chain transfer free energies (ΔGsc°) has historically not been well understood. A particularly challenging region for experimental interrogation is the bilayer interfacial region that is characterized by a steep polarity gradient. In this study, we have determined the ΔGsc° for nonpolar side chains as a function of bilayer position using a combination of experiment and simulation. We discovered an empirical correlation between the surface area of the nonpolar side chain, the transfer free energies, and the local water concentration in the

SUBMITTER: Marx DC 

PROVIDER: S-EPMC8634737 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature