Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix.

ABSTRACT: The transmembrane helices of membrane proteins often are flanked by interfacial charged or aromatic residues that potentially help to anchor the membrane-spanning protein. For isolated single-span helices, the interfacial residues may be especially important for stabilizing particular tilted transmembrane orientations. The peptide RWALP23 (acetyl-GR²ALW(LA)₆LWLAR²²A-amide) has been employed to investigate the interplay between interfacial arginines and tryptophans. Here we replace the tryptophans of RWALP23 with A5 and A19, to investigate arginines alone with respect to helix fraying and orientation in varying lipid bilayers. Deuterated alanines incorporated into the central sequence allow the orientation and stability of the core helix to be assessed by me

SUBMITTER: Sustich SJ 

PROVIDER: S-EPMC6943188 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature