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Nat Struct Biol. 2001 Jun;8(6):552-8.

Preorganized secondary structure as an important determinant of fast protein folding.

Author information

1
Department of Biochemistry, Box 3711, Duke University Medical Center, Durham, North Carolina 27710, USA.

Abstract

The folding and unfolding kinetics of the B-domain of staphylococcal protein A, a small three-helix bundle protein, were probed by NMR. The lineshape of a single histidine resonance was fit as a function of denaturant to give folding and unfolding rate constants. The B-domain folds extremely rapidly in a two-state manner, with a folding rate constant of 120,000 s-1, making it one of the fastest-folding proteins known. Diffusion-collision theory predicts folding and unfolding rate constants that are in good agreement with the experimental values. The apparent rate constant as a function of denaturant ('chevron plot') is predicted within an order of magnitude. Our results are consistent with a model whereby fast-folding proteins utilize a diffusion-collision mechanism, with the preorganization of one or more elements of secondary structure in the unfolded protein.

PMID:
11373626
DOI:
10.1038/88626
[Indexed for MEDLINE]

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