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

Guillaume Bouvignies, Pramodh Vallurupalli, D. Flemming Hansen, Bruno E. Correia, Oliver Lange, Alaji Bah, Robert M. Vernon, Frederick W. Dahlquist, David Baker and Lewis E. Kay ()
Additional contact information
Guillaume Bouvignies: The University of Toronto
Pramodh Vallurupalli: The University of Toronto
D. Flemming Hansen: The University of Toronto
Bruno E. Correia: University of Washington
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
Frederick W. Dahlquist: University of California Santa Barbara
David Baker: University of Washington
Lewis E. Kay: The University of Toronto

Nature, 2011, vol. 477, issue 7362, 111-114

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.

Date: 2011
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DOI: 10.1038/nature10349

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