On the combined analysis of ²H and ¹⁵N/¹H solid-state NMR data for determination of transmembrane peptide orientation and dynamics.

ABSTRACT: The dynamics of membrane-spanning peptides have a strong affect on the solid-state NMR observables. We present a combined analysis of ²H-alanine quadrupolar splittings together with ¹⁵N/(1)H dipolar couplings and ¹⁵N chemical shifts, using two models to treat the dynamics, for the systematic evaluation of transmembrane peptides based on the GWALP23 sequence (acetyl-GGALW(LA)₆LWLAGA-amide). The results indicate that derivatives of GWALP23 incorporating diverse guest residues adopt a range of apparent tilt angles that span 5°-35° in lipid bilayer membranes. By comparing individual and combined analyses of specifically ²H- or ¹⁵N-labeled peptides incorporated in magnetically or mechanically aligned lipid bilayers, we examine the influence of data-set size/identity, and of explicitly modeled d

SUBMITTER: Vostrikov VV 

PROVIDER: S-EPMC3244059 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature