This talk will focus on how dynamical properties and allostery vary across protein familes. Using our computational distance constraint model, our work has revealed that protein dynamics and allosteric mechanisms are extremely sensitive to even minimal perturbations. Typically, these perturbations lead to long-range effects that include unexpected increases in both flexibility and rigidity. Across whole protein families, this sensitivity can lead to dramatically different profiles. Yet, the observed differences are often related to the evolutionary distance between proteins. For example, we recently demonstrated in a statistically robust way that changes in allosteric couplings across the biomedically important β-lactamase enzyme family, while unrelated to substrate specificity, closely parallel the evolutionary history.<br/>

Entangled relationships: Protein flexibility, allostery, and mutation

253rd National Meeting (2017)

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