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

被引：0
作者：
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
机构：
[1] The University of Toronto,Department of Molecular Genetics
[2] The University of Toronto,Department of Biochemistry
[3] The University of Toronto,Department of Chemistry
[4] University of Washington,Department of Biochemistry
[5] Program in Computational Biology,Department of Chemistry and Biochemistry
[6] Instituto Gulbenkian de Ciência,undefined
[7] Hospital for Sick Children,undefined
[8] Program in Molecular Structure and Function,undefined
[9] 555 University Avenue,undefined
[10] University of California Santa Barbara,undefined
来源：
Nature | 2011年 / 477卷
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摘要：
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.
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页码：111 / 114
页数：3
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