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Correlated motions are a fundamental property of β-sheets

Author

Listed:
  • R. Bryn Fenwick

    (Joint BSC-CRG-IRB Research Programme in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona))

  • Laura Orellana

    (Joint BSC-CRG-IRB Research Programme in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona))

  • Santi Esteban-Martín

    (Joint BSC-CRG-IRB Research Programme in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona))

  • Modesto Orozco

    (Joint BSC-CRG-IRB Research Programme in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona)
    Departament de Bioquímica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona)

  • Xavier Salvatella

    (Joint BSC-CRG-IRB Research Programme in Computational Biology, Institute for Research in Biomedicine (IRB Barcelona)
    Institució Catalana de Recerca i Estudis Avançats (ICREA))

Abstract

Correlated motions in proteins can mediate fundamental biochemical processes such as signal transduction and allostery. The mechanisms that underlie these processes remain largely unknown due mainly to limitations in their direct detection. Here, based on a detailed analysis of protein structures deposited in the protein data bank, as well as on state-of-the art molecular simulations, we provide general evidence for the transfer of structural information by correlated backbone motions, mediated by hydrogen bonds, across β-sheets. We also show that the observed local and long-range correlated motions are mediated by the collective motions of β-sheets and investigate their role in large-scale conformational changes. Correlated motions represent a fundamental property of β-sheets that contributes to protein function.

Suggested Citation

  • R. Bryn Fenwick & Laura Orellana & Santi Esteban-Martín & Modesto Orozco & Xavier Salvatella, 2014. "Correlated motions are a fundamental property of β-sheets," Nature Communications, Nature, vol. 5(1), pages 1-9, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5070
    DOI: 10.1038/ncomms5070
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    Cited by:

    1. Dzmitry Ashkinadze & Harindranath Kadavath & Aditya Pokharna & Celestine N. Chi & Michael Friedmann & Dean Strotz & Pratibha Kumari & Martina Minges & Riccardo Cadalbert & Stefan Königl & Peter Günter, 2022. "Atomic resolution protein allostery from the multi-state structure of a PDZ domain," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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