Two-dimensional 1H-NMR investigation 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 sequencespecific 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 Cβ protons. A low-resolution three-dimensional structure of ribonuclease T1 was deduced from qualitative interpretation of long-range nuclear Overhauser effects. [ABSTRACT FROM AUTHOR]