Conformation of ribonuclease S-protein |
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| Authors: | H Shindo S Matsuura J S Cohen |
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| Institution: | (1) Developmental Pharmacology Branch and Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20014 Bethesda, Maryland, USA |
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| Abstract: | Summary 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. |
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