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 (tl/2~0.03 s) hydrophobic clusters and a compact state of the chain are formed. At the second stage (tl,'2 ~ 140 s) hydrophobic clusters are desolvated and the rigid native-like hydrophobic core is formed. At the third stage (tl/2 ~ 600 s) the native active protein is formed.

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