Cytochrome b 562 folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein
- 8 June 1999
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 96 (12) , 6587-6590
- https://doi.org/10.1073/pnas.96.12.6587
Abstract
Ferrocytochrome b 562 [Fe(II)cyt b 562 ] folding can be triggered by photoinduced electron transfer to unfolded Fe(III)cyt b 562 in 2–3 M guanidine hydrochloride solutions. The folding rates increase with decreasing guanidine hydrochloride; the extrapolated time constant for this folding process in the absence of denaturant (5 μs) is near the predicted value for intrachain diffusion. The relatively smooth energy landscape indicated for Fe(II)cyt b 562 folding accords with the helical, highly symmetrical structure of the protein.Keywords
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