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Slow equilibration of a denatured protein: comparison of the cluster model with the proline isomerization model
Authors:M I Kanehisa  T Y Tsong
Institution:Department of Physiological Chemistry The Johns Hopkins University School of Medicine Baltimore, Md 21205, U.S.A.
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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