Two-dimensional 1H-NMR investigation of ribonuclease T1. Resonance assignments, secondary and low-resolution tertiary structures of ribonuclease T1.
Ribonuclease T1 was studied by two-dimensional 1H-NMR spectroscopy. Resonance assignments were obtained for the backbone protons of 95 amino acid residues and most of its side-chain protons using sequence-specific assignment procedures. The secondary structure elements of ribonuclease T1 were identified by an investigation of medium- and long-range nuclear Overhauser effects between the backbone and C beta protons. A low-resolution three-dimensional structure of ribonuclease T1 was deduced from qualitative interpretation of long-range nuclear Overhauser effects.
D000595:Amino Acid Sequence; D000596:Amino Acids; D001236:Aspergillus oryzae / Q000201:enzymology; D004722:Endoribonucleases / Q000302:isolation & purification; D006859:Hydrogen; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D006163:Ribonuclease T1 / Q000302:isolation & purification
D000596:Amino Acids; D046911:Macromolecular Substances; D006859:Hydrogen; D004722:Endoribonucleases; D006163:Ribonuclease T1