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. 2013 Dec 10;11(Suppl 1):S2. doi: 10.1186/1477-3155-11-S1-S2

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Copyright © 2013 Schuler; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Nanosecond correlation spectroscopy used for the determination of unfolded state dynamics on the sub-microsecond timescale. (top) Cartoon of a FRET-labelled unfolded protein undergoing diffusive chain dynamics, resulting in fluctuations of the inter-dye distance, r(t) [12]. (bottom) Donor-donor (DD), acceptor-acceptor (AA), and donor-acceptor (DA) intensity correlation functions for an unfolded protein are shown (CspTm in 4 M GdmCl [96]) in the nanosecond range, where the decay at about 50 ns reports on the reconfiguration time of the polypeptide chain. Note that the donor-acceptor crosscorrelation shows anticorrelated behaviour, a signature of distance dynamics. Antibunching [112] occurs on the timescale of a few nanoseconds. Fits are shown as solid lines [96].