Abstract：
:Kinetic models were developed to describe the influence of prolyl peptide bond isomerization on the kinetics of reversible protein folding for cases in which structural intermediates do not occur. In the simulations, the number of prolyl residues and the relative rates of folding and isomerization were varied. The experimentally observed rate constants were found to be identical with the intrinsic rate constants of folding and isomerization only when folding remains much faster than prolyl isomerization throughout the transition region. When the rate of folding becomes similar to or lower than the rate of isomerization, the observed kinetic parameters are complex functions of all microscopic rate constants. In particular, the observed folding rates in the transition region decrease with the number of prolyl residues. Pseudo two-state kinetics with single folding and unfolding reactions are observed in several cases, although the apparent folding rates depend strongly on prolyl isomerization reactions in the unfolded chain. This virtual simplicity can easily lead to misinterpretation of kinetic data. Additional phases can be resolved when refolding is started from the fast-folding species (UF). The coupling between folding and prolyl peptide bond isomerization also modifies the dependence on denaturant concentration of the apparent rate constants of folding. We suggest several tests to detect and characterize the contributions of folding and isomerization steps to the observed folding kinetics.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Kiefhaber T,Kohler HH,Schmid FXdoi
10.1016/0022-2836(92)90585-8keywords:
subject
Has Abstractpub_date
1992-03-05 00:00:00pages
217-29issue
1eissn
0022-2836issn
1089-8638pii
0022-2836(92)90585-8journal_volume
224pub_type
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journal_title：Journal of molecular biology
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pub_type： 杂志文章,评审
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pub_type： 杂志文章
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更新日期：1993-12-20 00:00:00
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更新日期：1989-10-20 00:00:00
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更新日期：2003-11-21 00:00:00
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