On the Dynamic Origins of Allosteric Activation

doi:10.1126/science.293.5534.1397p

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Using nuclear magnetic resonance measurements, Volkman et al. (Reports, 23 March 2001, p. 2429) found "a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics." These results, they suggested, imply that functionally important protein motions are likely to be in the millisecond-to-microsecond time regime, because many biological processes occur on that time scale. Wand comments that the Volkman et al. study, while reporting "exciting results," inappropriately "discounted an allosteric role for subnanosecond motion" and did not sufficiently acknowledge the potential role of fast side-chain motion as "a contributor to allosteric free energy transduction in proteins." Kern responds that the concepts raised by Wand "are fundamental principles of protein biochemistry with which we have no disagreement," and that "neither our results nor our conclusions are discordant with the issues discussed by Wand." The full text of these comments can be seen at www.sciencemag.org/cgi/content/full/293/5534/1395a.