Please use this identifier to cite or link to this item: https://doi.org/10.1006/jmbi.1997.1043
Title: Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2
Authors: Tan, Y.-J. 
Oliveberg, M.
Otzen, D.E.
Fersht, A.R.
Keywords: cis-trans
Folding
Protein
Issue Date: 20-Jun-1997
Citation: Tan, Y.-J., Oliveberg, M., Otzen, D.E., Fersht, A.R. (1997-06-20). Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. Journal of Molecular Biology 269 (4) : 611-622. ScholarBank@NUS Repository. https://doi.org/10.1006/jmbi.1997.1043
Abstract: There are four peptidyl-proline bonds in the 64-residue protein chymotrypsin inhibitor 2 (CI2), all of which are in the trans conformation in the native structure. The isomerisation of one or more of these peptidyl-proline bonds to the cis conformation in the denatured state gives rise to heterogeneity, leading to both fast and slow-folding species. The refolding of the fast-folding species, which has all trans peptidyl-proline bonds, is much faster than that of the slow-folding species, which have one or more cis peptidyl-proline bonds. In CI2, the slow-folding species can be classified into two groups by their rates of refolding, temperature-dependence, pH-dependence and [GdmCl]-dependence of the rate constants and the effect of peptidyl-prolyl isomerase on the rate constants. The replacement of Pro6 by Ala removes one of the slow refolding phases, suggesting that the cis peptidyl-Pro6 conformation is solely responsible for one of the slow-folding species. Pro6 is located in a region of the protein where non-random interactions have been found in a series of N-terminal fragments of CI2 (residues 1 to 13, 1 to 25, 1 to 28 and 1 to 40). In addition, NMR studies on a mutant fragment, (1-40)T3A, have confirmed that this non-native interaction is associated with the bulky side-chain of Trp5. The atypical rate of cis to trans isomerisation of the peptidyl-Pro bond is indicative of the presence of a similar hydrophobic cluster in the physiological denatured state of intact CI2.
Source Title: Journal of Molecular Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/112038
ISSN: 00222836
DOI: 10.1006/jmbi.1997.1043
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