Techniques and applications of NMR to membrane proteins.
The fact that membrane proteins are notoriously difficult to analyse using standard protocols for atomic-resolution structure determination methods have motivated adaptation of these techniques to membrane protein studies as well as development of new technologies. With this motivation, liquid-state nuclear magnetic resonance (NMR) has recently been used with success for studies of peptides and membrane proteins in detergent micelles, and solid-state NMR has undergone a tremendous evolution towards characterization of membrane proteins in native membrane and oriented phospholipid bilayers. In this mini-review, we describe some of the technological challenges behind these efforts and provide examples on their use in membrane biology.
Nielsen
Nielschr
N
Department of Chemistry, University of Aarhus, Aarhus C, Denmark. ncn@chem.au.dk
Malmendal
Anders
A
Vosegaard
Thomas
T
D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation
D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D001436:Bacteriorhodopsins