期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：10
页码：4764-4768
DOI：10.1073/pnas.75.10.4764
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Unfolded RNase A is known to contain an equilibrium mixture of two forms, a slow-folding form (U1) and a fast-folding form (U2). If U1 is produced after unfolding by the slow cis-trans isomerization of proline residues about X-Pro imide bonds, then the formation of U1 should be catalyzed by strong acids. Therefore, the rate of formation of U1 has been measured at different HClO4 concentrations. After rapid unfolding of the native protein in concentrated HClO4 at 0{degrees
