Sequential mechanism of refolding of carbonic anhydrase B
- 16 November 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 224 (1), 9-13
- https://doi.org/10.1016/0014-5793(87)80412-x
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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