Slow equilibration of a denatured protein: comparison of the cluster model with the proline isomerization model |
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| Authors: | M I Kanehisa T Y Tsong |
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| Affiliation: | Department of Physiological Chemistry The Johns Hopkins University School of Medicine Baltimore, Md 21205, U.S.A. |
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| Abstract: | ![]()
The slow equilibration of the denatured state after rapid unfolding of a globular protein is examined by the cluster model of protein folding (Kanehisa &; Tsong, 1978). The detection of this process in ribonuclease A and its acid catalysis have been considered evidence for the proline isomerization model. Our calculation shows that similar kinetic behavior is also expected for the cluster model. |
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