Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family

Beth G. Wensley, Sarah Batey, Fleur A. C. Bone, Zheng Ming Chan, Nuala R. Tumelty, Annette Steward, Lee Gyan Kwa, Alessandro Borgia and Jane Clarke ()
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Beth G. Wensley: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Sarah Batey: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Fleur A. C. Bone: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Zheng Ming Chan: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Nuala R. Tumelty: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Annette Steward: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Lee Gyan Kwa: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Alessandro Borgia: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK
Jane Clarke: University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK

Nature, 2010, vol. 463, issue 7281, 685-688

Abstract: Funnel vision: putting a brake on protein folding Protein folding is commonly pictured as a slide down the slopes of a free-energy landscape or 'folding funnel'. Theory predicts that the roughness of such slopes — resulting from local energy traps — should slow folding. Wensley et al. confirm this prediction by demonstrating that the internal friction of preformed helices does cause some members of the 'spectrin' domain family to fold (or unfold) 3,000 times more slowly than others. The authors propose that this unusual feature might have evolved to make spectrins last longer without turnover in red blood cells.

Date: 2010
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DOI: 10.1038/nature08743

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