Conformation of ribonuclease S-protein.
Ribonuclease S-protein exhibits a pH-dependent conformational transition between folded and unfolded states, and some unfolded S-protein persists up to pH 8. The histidine C2 proton resonance of the unfolded species was erroneously assigned by Bradbury et al. to histidine residue 119 of the folded species.
D006639:Histidine / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012260:Ribonucleases
D046911:Macromolecular Substances; D006639:Histidine; D012260:Ribonucleases; C022542:ribonuclease S