title: Techniques and applications of NMR to membrane proteins.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Aarhus, Aarhus C, Denmark. ncn@chem.au.dk
authors.forename: Nielschr
authors.initials: N
authors.lastname: Nielsen
authors.forename: Anders
authors.initials: A
authors.lastname: Malmendal
authors.forename: Thomas
authors.initials: T
authors.lastname: Vosegaard
mesh_terms: 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
chemical_list: D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D001436:Bacteriorhodopsins