Abstract

In this review we describe how the properties of cellular membranes govern protein structure and activity. Lipids can modulate protein functional states through general bilayer properties, or by specific binding and acting as allosteric regulators. Hydrophobic matching by solvation of the protein surface entails short-range interactions of the lipids, and cellular water affects bilayer structure through hydrating the lipid polar head groups and protein hydrophilic domains. Biomembranes have important analogies to supercritical fluids leading to raft-like nanostructures with cholesterol. Additional long-range interactions of the lipids and proteins involve the curvature stress field, where a flexible surface model (FSM) describes how collective properties of the lipids affect the conformational energetics of membrane proteins. Curvature elasticity and hydrophobicity of native lipid mixtures play key roles in functional proteolipid couplings and give insights into protein activation mechanisms in cellular membranes.

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