Mutational scanning reveals the determinants of protein insertion and association energetics in the plasma membrane.

ABSTRACT: Insertion of helix-forming segments into the membrane and their association determines the structure, function, and expression levels of all plasma membrane proteins. However, systematic and reliable quantification of membrane-protein energetics has been challenging. We developed a deep mutational scanning method to monitor the effects of hundreds of point mutations on helix insertion and self-association within the bacterial inner membrane. The assay quantifies insertion energetics for all natural amino acids at 27 positions across the membrane, revealing that the hydrophobicity of biological membranes is significantly higher than appreciated. We further quantitate the contributions to membrane-protein insertion from positively charged residues at the cytoplasm-membrane interface and reve

SUBMITTER: Elazar A 

PROVIDER: S-EPMC4786438 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature