Determination of the conformations of bound peptides using NMR-transferred nOe techniques.
NMR-transferred nOe spectroscopy provides a means for determining the structure of a peptide bound to a macromolecular target when the complex is too large to be studied by conventional NMR techniques. Recent examples of structures that have been determined by NMR-transferred nOe techniques include platelet-receptor peptide bound to thrombin, cholera toxin peptide bound to antibodies, troponin I peptide bound to troponin C and the vsv-C peptide bound to chaperones DnaK and GroEL.
Sykes
B D
BD
Department of Biochemistry, University of Alberta, Edmonton, Canada.
D000595:Amino Acid Sequence; D000818:Animals; D001709:Biotechnology; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
D010455:Peptides