Article
Key role of coulombic interactions for the folding transition state of the cold shock protein.
Journal of molecular biology - 1 Dec 2006
Garcia-Mira Maria M, Schmid Franz X
Abstract excerpt
The cold shock protein CspB shows a five-stranded beta-sheet structure, and it folds rapidly via a native-like transition state. A previous Phi value analysis showed that most of the residues with Phi values close to one reside in strand beta1, and two of them, Lys5 and Lys7 are partially exposed charged residues. To elucidate how coulombic interactions of these two residues contribute to the energetic...
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