Statistically derived asymmetric membrane potentials from α-helical and β-barrel membrane proteins.

ABSTRACT: Modeling membrane protein (MP) folding, insertion, association and their interactions with other proteins, lipids, and drugs requires accurate transfer free energies (TFEs). Various TFE scales have been derived to quantify the energy required or released to insert an amino acid or protein into the membrane. Experimental measurement of TFEs is challenging, and only few scales were extended to depth-dependent energetic profiles. Statistical approaches can be used to derive such potentials; however, this requires a sufficient number of MP structures. Furthermore, MPs are tightly coupled to bilayers that are heterogeneous in terms of lipid composition, asymmetry, and protein content between organisms and organelles. Here we derived asymmetric implicit membrane potentials from β-barrel and α-he

SUBMITTER: Koehler Leman J 

PROVIDER: S-EPMC5849751 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature