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

Author

Listed:
  • 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
    Current addresses: Covagen AG, c/o ETH Zürich, Y17 M22, Life Science ETH/Uni, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland (S.B.); Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland (A.B.).)

  • 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
    Current addresses: Covagen AG, c/o ETH Zürich, Y17 M22, Life Science ETH/Uni, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland (S.B.); Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland (A.B.).)

  • Jane Clarke

    (University of Cambridge, MRC Centre for Protein Engineering, Lensfield Rd, Cambridge CB2 1EW UK)

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.

Suggested Citation

  • Beth G. Wensley & Sarah Batey & Fleur A. C. Bone & Zheng Ming Chan & Nuala R. Tumelty & Annette Steward & Lee Gyan Kwa & Alessandro Borgia & Jane Clarke, 2010. "Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family," Nature, Nature, vol. 463(7281), pages 685-688, February.
    • Handle: RePEc:nat:nature:v:463:y:2010:i:7281:d:10.1038_nature08743
    DOI: 10.1038/nature08743
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    Cited by:

    1. Yunxiang Sun & Dengming Ming, 2014. "Energetic Frustrations in Protein Folding at Residue Resolution: A Homologous Simulation Study of Im9 Proteins," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-11, January.

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