Predicting interfacial partitioning into zwitterionic and anionic membranes

Abstract

Transitions of soluble proteins into lipid membranes are crucial for numerous physiological processes, including apoptotic regulation, neurodegeneration, and bacterial infections. In many cases, conformational switching during such transitions is initiated by changes in the protonation state of titratable residues. Our ability to predict these transitions is currently limited by knowledge gaps in the thermodynamics of protein-membrane interactions, especially in the presence of anionic lipids. Predictions of protein-membrane interactions and topology of inserted proteins often utilize hydropathy plots.