[NMR spectroscopy in the study of the spatial structure of membrane peptides and proteins].
The review covers the field of the spatial structure determination of membrane-associated peptides and proteins by the High-Resolution NMR Spectroscopy. The membrane-bound conformations of several hormones, neuropeptides, lipopeptides, peptide antibiotics, bacteriophage coat proteins, transmembrane domains of receptors and others are considered. To mimic the biomembrane environment the appropriate artificial media (organic solvents, micelles of detergents of lipid vesicles) must be adjusted. In that case NMR spectroscopy is a powerful tool for the spatial structure and dynamics investigations of membrane associated peptides and proteins constituting the bases for unraveling of their structure-function relationships.
Pervushin
K V
KV
Arsen'ev
A S
AS
D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D008565:Membrane Proteins; D010455:Peptides
Spektroskopiia IaMR v issledovaniiakh prostranstvennoĭ struktury membrannykh peptidov i belkov.