Sequential mechanism of refolding of carbonic anhydrase B
Authors:
- Gennady V. SemisotnovGennady V. Semisotnov
- Natalya A. RodionovaNRNatalya A. Rodionova
- Victor P. KutyshenkoVKVictor P. Kutyshenko
- Bernd EbertBEBernd Ebert
- Jürgen BlanckJBJürgen Blanck
- Oleg B. PtitsynOPOleg B. Ptitsyn
- 16 November 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 224 (1) , 9-13
Abstract
The kinetics of refolding of bovine carbonic anhydrase B was studied by a variety of methods over a wide range of times (from milliseconds to hours). It has been shown that protein refolding proceeds through three stages. At the first stage (t ½≈0.03 s) hydrophobic clusters and a compact state of the chain are formed. At the second stage (t ½≈140 s) hydrophobic clusters are desolvated and the rigid native‐like hydrophobic core is formed. At the third stage (t ½≈600 s) the native active protein is formed.Keywords
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