Secondary structure of the alpha-amylase polypeptide inhibitor tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance.
Complete sequence-specific 1H nuclear magnetic resonance assignments were obtained for the backbone hydrogen atoms in Tendamistat, a protein with 74 residues. From NOESY observation of 1H-1H short distance constraints, measurements of the spin-spin couplings 3JHN alpha and a qualitative identification of slowly exchanging amide protons, two antiparallel beta-sheets containing three and four strands, respectively, were identified. The peptide segments outside the beta-sheets do not form regular secondary structure. Preliminary data were obtained on the relative spatial arrangements of the two beta-sheets.
D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides; D011487:Protein Conformation; D012996:Solutions; D013302:Streptomyces / Q000032:analysis*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*
D010455:Peptides; D012996:Solutions; D000516:alpha-Amylases; C030526:tendamistate