Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR

J Biomol NMR. 2004 Nov;30(3):253-65. doi: 10.1007/s10858-004-3452-3.

Abstract

One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides under Magic Angle Spinning. The functional dependence of a series of anisotropic recoupling schemes is analyzed using theoretical and numerical methods. These studies lead to the construction of a set of polarization dephasing or transfer units that probe local backbone conformation and overall molecular orientation within the same NMR experiment. Experimental results are shown for a randomly oriented peptide and for two model membrane-peptides reconstituted into lipid bilayers and oriented on polymer films according to a method proposed by Bechinger et al.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anisotropy
  • Gramicidin / chemistry*
  • Lipid Bilayers / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Peptides / chemistry*
  • Spin Labels

Substances

  • Lipid Bilayers
  • Peptides
  • Spin Labels
  • Gramicidin