Abstract:Protein functions result from local and collective atomic motions that span a wide range of time scales. An integrated analysis of experimental and simulation data can shed light on the detailed mechanism of these motions. Applying a high electric field to protein crystals enables conformational changes that can be captured by time-resolved X-ray crystallography. Such an experiment (referred to as EF-X) carried out on a human PDZ domain obtained a series of atomistic ''snapshots'' of ensemble averages protein … Show more
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