Extremely rapid protein folding in the absence of intermediates.


Here we used the cold-shock protein CspB from Bacillus subtilis to study protein folding at an elementary level. The thermodynamic stability of this small five-stranded beta-barrel protein is low, but unfolding and refolding are extremely rapid reactions. In 0.6 M urea the time constant of refolding is about 1.5 ms, and at the transition midpoint (4 M urea) the folded and unfolded forms equilibrate in less than 100 ms. Both the equilibrium unfolding transition and the folding kinetics are perfectly described by a N<-->U two-state model. The validity of this model was confirmed by several kinetic tests. Folding intermediates could neither be detected at equilibrium nor in the folding kinetics. We suggest that the extremely rapid folding of CspB and the absence of folding intermediates are related phenomena. Study holds ProTherm entries: 9329 Extra Details: cold-shock protein CspB; thermodynamic stability;,time constant of refolding; folding intermediates

Submission Details

ID: Z8QdExir3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:37 p.m.

Version: 1

Publication Details
Schindler T;Herrler M;Marahiel MA;Schmid FX,Nat. Struct. Biol. (1995) Extremely rapid protein folding in the absence of intermediates. PMID:7552728
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