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 dynamics, on the deduced average orientations of the peptides. We conclude that peptides with small apparent tilt values (\\textless\∼10°) can be fitted by extensive families of solutions, which can be narrowed by incorporating additional ¹⁵N as well as ²H restraints. Conversely, peptides exhibiting larger tilt angles display more narrow distributions of tilt and rotation that can be fitted using smaller sets of experimental constraints or even with ²H or ¹⁵N data alone. Importantly, for peptides that tilt significantly more than 10° from the bilayer-normal, the contribution from rigid body dynamics can be approximated by a principal order parameter.
%0 Journal Article
%1 vostrikov_combined_2011
%A Vostrikov, Vitaly V
%A Grant, Christopher V
%A Opella, Stanley J
%A Koeppe, Roger E
%D 2011
%J Biophys. J.
%K Chemical,Computer Isotopes,Protons,Structure-Activity Proteins,Models,Molecular,Nitrogen Relationship Resonance Simulation,Hydrogen,Lipid Spectroscopy,Membrane bilayers,Magnetic
%N 12
%P 2939--2947
%R 10.1016/j.bpj.2011.11.008
%T On the combined analysis of ²\H\ and ¹⁵\N\/¹\H\ solid-state \NMR\ data for determination of transmembrane peptide orientation and dynamics
%V 101
%X 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 dynamics, on the deduced average orientations of the peptides. We conclude that peptides with small apparent tilt values (\\textless\∼10°) can be fitted by extensive families of solutions, which can be narrowed by incorporating additional ¹⁵N as well as ²H restraints. Conversely, peptides exhibiting larger tilt angles display more narrow distributions of tilt and rotation that can be fitted using smaller sets of experimental constraints or even with ²H or ¹⁵N data alone. Importantly, for peptides that tilt significantly more than 10° from the bilayer-normal, the contribution from rigid body dynamics can be approximated by a principal order parameter.
@article{vostrikov_combined_2011,
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 dynamics, on the deduced average orientations of the peptides. We conclude that peptides with small apparent tilt values ({\{}{\textless}{\}}∼10°) can be fitted by extensive families of solutions, which can be narrowed by incorporating additional ¹⁵N as well as ²H restraints. Conversely, peptides exhibiting larger tilt angles display more narrow distributions of tilt and rotation that can be fitted using smaller sets of experimental constraints or even with ²H or ¹⁵N data alone. Importantly, for peptides that tilt significantly more than 10° from the bilayer-normal, the contribution from rigid body dynamics can be approximated by a principal order parameter.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Vostrikov, Vitaly V and Grant, Christopher V and Opella, Stanley J and Koeppe, Roger E},
biburl = {https://www.bibsonomy.org/bibtex/27d06a985e72a0eb3385c79718d7342dd/nmrresource},
doi = {10.1016/j.bpj.2011.11.008},
interhash = {ff31eeb8f3ddaefd184f2e733599afe3},
intrahash = {7d06a985e72a0eb3385c79718d7342dd},
issn = {1542-0086},
journal = {Biophys. J.},
keywords = {Chemical,Computer Isotopes,Protons,Structure-Activity Proteins,Models,Molecular,Nitrogen Relationship Resonance Simulation,Hydrogen,Lipid Spectroscopy,Membrane bilayers,Magnetic},
month = dec,
number = 12,
pages = {2939--2947},
pmid = {22208192},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{On the combined analysis of ²{\{}H{\}} and ¹⁵{\{}N{\}}/¹{\{}H{\}} solid-state {\{}NMR{\}} data for determination of transmembrane peptide orientation and dynamics}},
volume = 101,
year = 2011
}