Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy

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DOIResolve DOI: http://doi.org/10.1038/ncomms2204
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TypeArticle
Journal titleNature Communications
ISSN2041-1723
Volume3
Article number1195
AbstractTheory, simulations and experimental results have suggested an important role of internal friction in the kinetics of protein folding. Recent experiments on spectrin domains provided the first evidence for a pronounced contribution of internal friction in proteins that fold on the millisecond timescale. However, it has remained unclear how this contribution is distributed along the reaction and what influence it has on the folding dynamics. Here we use a combination of single-molecule Förster resonance energy transfer, nanosecond fluorescence correlation spectroscopy, microfluidic mixing and denaturant- and viscosity-dependent protein-folding kinetics to probe internal friction in the unfolded state and at the early and late transition states of slow- and fast-folding spectrin domains. We find that the internal friction affecting the folding rates of spectrin domains is highly localized to the early transition state, suggesting an important role of rather specific interactions in the rate-limiting conformational changes.
Publication date
LanguageEnglish
AffiliationNational Institute for Nanotechnology; National Research Council Canada
Peer reviewedYes
NPARC number21268918
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Record identifier1da9f759-09e0-4023-86c7-0456fffa8971
Record created2013-11-25
Record modified2016-05-09
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