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Solution structure of a minor and transiently formed state of a T4 lysozyme mutant

Author

Listed:
  • Guillaume Bouvignies

    (The University of Toronto
    The University of Toronto
    The University of Toronto)

  • Pramodh Vallurupalli

    (The University of Toronto
    The University of Toronto
    The University of Toronto)

  • D. Flemming Hansen

    (The University of Toronto
    The University of Toronto
    The University of Toronto)

  • Bruno E. Correia

    (University of Washington
    Program in Computational Biology, Instituto Gulbenkian de Ciência)

  • Oliver Lange

    (University of Washington)

  • Alaji Bah

    (Hospital for Sick Children, Program in Molecular Structure and Function, 555 University Avenue)

  • Robert M. Vernon

    (University of Washington
    Hospital for Sick Children, Program in Molecular Structure and Function, 555 University Avenue)

  • Frederick W. Dahlquist

    (University of California Santa Barbara)

  • David Baker

    (University of Washington)

  • Lewis E. Kay

    (The University of Toronto
    The University of Toronto
    The University of Toronto
    Hospital for Sick Children, Program in Molecular Structure and Function, 555 University Avenue)

Abstract

Structure of a protein intermediate The function of a protein depends critically on structural dynamics, and on the nature of the transient conformation intermediates that the molecule can adopt. These transients can be elusive and therefore hard to characterize. This paper reports the use of a combination of relaxation-dispersion nuclear magnetic resonance with Rosetta computational structure predictions to design T4 lysozyme mutations that stabilize 'excited' states that are normally too transient to be observed.

Suggested Citation

  • Guillaume Bouvignies & Pramodh Vallurupalli & D. Flemming Hansen & Bruno E. Correia & Oliver Lange & Alaji Bah & Robert M. Vernon & Frederick W. Dahlquist & David Baker & Lewis E. Kay, 2011. "Solution structure of a minor and transiently formed state of a T4 lysozyme mutant," Nature, Nature, vol. 477(7362), pages 111-114, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7362:d:10.1038_nature10349
    DOI: 10.1038/nature10349
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    Cited by:

    1. Kalyan S. Chakrabarti & Simon Olsson & Supriya Pratihar & Karin Giller & Kerstin Overkamp & Ko On Lee & Vytautas Gapsys & Kyoung-Seok Ryu & Bert L. Groot & Frank Noé & Stefan Becker & Donghan Lee & Th, 2022. "A litmus test for classifying recognition mechanisms of transiently binding proteins," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Tobias Sikosek & Heinrich Krobath & Hue Sun Chan, 2016. "Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches," PLOS Computational Biology, Public Library of Science, vol. 12(6), pages 1-27, June.
    3. Tobias Sikosek & Erich Bornberg-Bauer & Hue Sun Chan, 2012. "Evolutionary Dynamics on Protein Bi-stability Landscapes can Potentially Resolve Adaptive Conflicts," PLOS Computational Biology, Public Library of Science, vol. 8(9), pages 1-17, September.

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