Electric-field-stimulated protein mechanics

Doeke R. Hekstra, K. Ian White, Michael A. Socolich, Robert W. Henning, Vukica Šrajer and Rama Ranganathan ()
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Doeke R. Hekstra: Green Center for Systems Biology, UT Southwestern Medical Center
K. Ian White: Green Center for Systems Biology, UT Southwestern Medical Center
Michael A. Socolich: Green Center for Systems Biology, UT Southwestern Medical Center
Robert W. Henning: Center for Advanced Radiation Sources, The University of Chicago
Vukica Šrajer: Center for Advanced Radiation Sources, The University of Chicago
Rama Ranganathan: Green Center for Systems Biology, UT Southwestern Medical Center

Nature, 2016, vol. 540, issue 7633, 400-405

Abstract: Abstract The internal mechanics of proteins—the coordinated motions of amino acids and the pattern of forces constraining these motions—connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2PDZ2) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function.

Date: 2016
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DOI: 10.1038/nature20571

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