Influence of glutamic acid residues and pH on the properties of transmembrane helices.

ABSTRACT: Negatively charged side chains are important for the function of particular ion channels and certain other membrane proteins. To investigate the influence of single glutamic acid side chains on helices that span lipid-bilayer membranes, we have employed GWALP23 (acetyl-GGALW⁵LALALALALALALW¹⁹LAGA-amide) as a favorable host peptide framework. We substituted individual Leu residues with Glu residues (L12E or L14E or L16E) and incorporated specific ²H-labeled alanine residues within the core helical region or near the ends of the sequence. Solid-state ²H NMR spectra reveal little change for the core labels in GWALP23-E12, -E14 and -E16 over a pH range of 4 to 12.5, with the spectra being broader for samples in DOPC compared to DLPC bilayers. The spec

SUBMITTER: Rajagopalan V 

PROVIDER: S-EPMC5274556 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature