Transmembrane Helix Integrity versus Fraying To Expose Hydrogen Bonds at a Membrane-Water Interface.

ABSTRACT: Transmembrane helices dominate the landscape for many membrane proteins. Often flanked by interfacial aromatic residues, these transmembrane helices also contain loops and interhelix segments, which could help in stabilizing a transmembrane orientation. Using ²H nuclear magnetic resonance spectroscopy to monitor bilayer-incorporated model GWALP23 family peptides, we address systematically the issue of helix fraying in relation to the dynamics and orientation of highly similar individual transmembrane helices. We inserted aromatic (Phe, Trp, Tyr, and His) or non-aromatic residues (Ala and Gly) into positions 4 and 5 adjacent to a core transmembrane helix to examine the side-chain dependency of the transmembrane orientation, dynamics, and helix integrity (extent and location of un

SUBMITTER: Afrose F 

PROVIDER: S-EPMC6372336 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature