Primary Peptide Folding Dynamics Observed with Ultrafast Temperature Jump
An ultrafast laser temperature jump (T-jump) induces folding and unfolding of Wh5 (see picture), the shortest possible α-helical peptide. Using time-resolved fluorescence spectroscopy, the folding time of this peptide was found to span from less than one nanosecond to a few nanoseconds, redefining the meaning of ultrafast dynamics in protein and peptide folding.
Additional InformationCopyright © 2009 WILEY-VCH. Received: 27 January 2009; Revised: 11 March 2009. Published Online: 20 April 2009. We are grateful to the National Science Foundation and National Institutes of Health for funding of this research at Caltech. M.M.L. acknowledges financial support from the Krell Institute and the US Department of Energy (DoE) for a graduate fellowship at Caltech. We thank Dr. Dmitry Shorokhov for his effort in establishing the needed computation facility and for stimulating discussions. We also acknowledge the technical assistance of Drs. Hairong Ma and Chaozhi Wan in the laser T-jump setup. G.S.J. gratefully acknowledges Krzysztof Kuczera and William Eaton for helpful discussion.
Accepted Version - nihms149085.pdf
Supplemental Material - sm001.pdf