Conformation of ribonuclease S-protein
Copyright policy ) H, Shindo; S, Matsuura; J S, Cohen;
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.
- National Institute of Health Pakistan
- National Institutes of Health United States
Magnetic Resonance Spectroscopy, Ribonucleases, Macromolecular Substances, Protein Conformation, Histidine, Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy, Ribonucleases, Macromolecular Substances, Protein Conformation, Histidine, Hydrogen-Ion Concentration
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