Atom-scale models by Rice University scientists based on those used to predict how proteins fold show a strong correlation between minimally frustrated binding sites and drug specificity. The funnel, a visual representation of the protein’s energy landscape as it folds, helps locate those frustrated sites. Such models could lead to better-designed drugs with fewer side effects. Illustration by Mingchen Chen
Atom-scale models by Rice University scientists based on those used to predict how proteins fold show a strong correlation between minimally frustrated binding sites and drug specificity. The funnel, a visual representation of the protein's energy landscape as it folds, helps locate those frustrated sites. Such models could lead to better-designed drugs with fewer side effects. Illustration by Mingchen Chen - Rice scientists' atomic resolution protein models reveal new details about protein binding Knowing precisely where proteins are frustrated could go a long way toward making better drugs. That's one result of a new study by Rice University scientists looking for the mechanisms that stabilize or destabilize key sections of biomolecules. Atom-scale models by Rice theorist Peter Wolynes , lead author and alumnus Mingchen Chen and their colleagues at the Center for Theoretical Biological Physics show that not only are some specific frustrated sequences in proteins necessary to allow them to function, locating them also offers clues to achieve better specificity for drugs. That knowledge could also help design drugs with fewer side effects, Wolynes said.
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