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

Abstract：

:Theory, 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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Borgia A,Wensley BG,Soranno A,Nettels D,Borgia MB,Hoffmann A,Pfeil SH,Lipman EA,Clarke J,Schuler B

doi

10.1038/ncomms2204

subject

Has Abstract

pub_date

2012-01-01 00:00:00

pages

1195

issn

2041-1723

pii

ncomms2204

journal_volume

3

pub_type

杂志文章

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