Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds.
作者： C N Pace , G R Grimsley , J A Thomson , B J Barnett
DOI: 10.1016/S0021-9258(18)37859-1
关键词: Side chain 、 Conformational entropy 、 Chemistry 、 Ribonuclease T1 、 Urea 、 RNase P 、 Stereochemistry 、 Cysteine 、 Molecule 、 Crystallography 、 Protein structure
摘要: … It will be interesting to see how the mechanism of folding is influenced by these changes in the conformational stability and by changes in the number of the disulfide bonds. Studies of …
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