Extremely rapid protein folding in the absence of intermediates.
Abstract
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:7552728Additional Information
Study Summary
| Number of data points | 1 |
| Proteins | Cold shock protein CspB ; Cold shock protein CspB |
| Unique complexes | 1 |
| Assays/Quantities/Protocols | Experimental Assay: dG_H2O |
| Libraries | Mutations for sequence MLEGKVKWFNSEKGFGFIEVEGQDDVFVHFSAIQGEGFKTLEEGQAVSFEIVEGNRGPQAANVTKEA |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
|---|
Data Distribution
Studies with similar sequences (approximate matches)