Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the alpha-amylase inhibitor tendamistat.
This is a preliminary report on the determination of the solution conformation of the alpha-amylase inhibitor Tendamistat by nuclear magnetic resonance and distance geometry calculations. A characterization is given of the complete polypeptide backbone fold and the side-chains of the presumed active site in this protein. These results are based on complete sequence-specific resonance assignments, a list of 401 distance constraints from nuclear Overhauser effects, 168 distance constraints from hydrogen bonds and disulphide bridges, and 50 torsion angle constraints from measurements of spin-spin coupling constants.
D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides; D011487:Protein Conformation; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D010455:Peptides; D000516:alpha-Amylases; C030526:tendamistate