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J Magn Reson. 2014 Mar;240:34-44. doi: 10.1016/j.jmr.2013.12.014. Epub 2014 Jan 21.

Assignment of oriented sample NMR resonances from a three transmembrane helix protein.

Author information

  • 1Institute for Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA; National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA.
  • 2National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA.
  • 3Institute for Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA; National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA; Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, USA. Electronic address: cross@magnet.fsu.edu.

Abstract

Oriented sample solid state NMR techniques have been routinely employed to determine the structures of membrane proteins with one or two transmembrane helices. For larger proteins the technique has been limited by spectral resolution and lack of assignment strategies. Here, a strategy for resonance assignment is devised and applied to a three transmembrane helix protein. Sequence specific assignments for all labeled transmembrane amino acid sites are obtained, which provide a set of orientational restraints and helix orientations in the bilayer. Our experiments expand the utility of solid state NMR in membrane protein structure characterization to three transmembrane helix proteins and represent a straightforward strategy for routinely characterizing multiple transmembrane helix protein structures.

Copyright © 2014 Elsevier Inc. All rights reserved.

KEYWORDS:

Helix orientation; Lipid bilayer; Membrane protein; Membrane protein structure; Mycobacterium tuberculosis; Oriented sample solid state NMR; Resonance assignment

PMID:
24509383
[PubMed - indexed for MEDLINE]
PMCID:
PMC3980497
Free PMC Article
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