Abstract：
:Kinetics of refolding of bovine carbonic anhydrase B have been studied by the "double-jump" technique (i.e. the dependence of protein refolding on delay time in the unfolded state after fast unfolding). It is shown that two stages (the slow with a relaxation time of t1/2 approximately equal to 120 s and the superslow with t1/2 approximately equal to 600 s) observed during refolding of bovine carbonic anhydrase B are due to trans-cis isomerization of proline residues. The dependences of rate constants of these processes on temperature and on the final denaturant concentration were measured. Activation energies of both processes are the same, Ea = 18(+/- 2) kcal/mol. The rate constants of protein refolding do not depend on the final concentration of urea under native conditions. In addition, the rate of isomerization of essential proline residues in the "molten globule" intermediate state of bovine carbonic anhydrase was measured and found to be equal to that for unstructural polypeptides. The effect of several proline residues on carbonic anhydrase refolding is discussed.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Semisotnov GV,Uversky VN,Sokolovsky IV,Gutin AM,Razgulyaev OI,Rodionova NAdoi
10.1016/S0022-2836(05)80215-3subject
Has Abstractpub_date
1990-06-05 00:00:00pages
561-8issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(05)80215-3journal_volume
213pub_type
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journal_title：Journal of molecular biology
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journal_title：Journal of molecular biology
pub_type： 杂志文章
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