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

Alessandro Borgia, Beth G. Wensley, Andrea Soranno, Daniel Nettels, Madeleine B. Borgia, Armin Hoffmann, Shawn H. Pfeil, Everett A. Lipman, Jane Clarke and Benjamin Schuler ()
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Alessandro Borgia: University of Zurich
Beth G. Wensley: University of Cambridge Chemical Laboratory
Andrea Soranno: University of Zurich
Daniel Nettels: University of Zurich
Madeleine B. Borgia: University of Zurich
Armin Hoffmann: University of Zurich
Shawn H. Pfeil: University of California
Everett A. Lipman: University of California
Jane Clarke: University of Cambridge Chemical Laboratory
Benjamin Schuler: University of Zurich

Nature Communications, 2012, vol. 3, issue 1, 1-9

Abstract: 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.

Date: 2012
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DOI: 10.1038/ncomms2204

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