Wobbles and Quivers of Proteins Play a Critical Role in Their Ability to Function
Updated: Aug 4
Johns Hopkins Medicine scientists report that they have probed the atomic structure of proteins to add evidence to the notion that the wobbles, shakes and quivers of proteins play a critical role in their ability to function. The research findings, the team says, may help scientists design new drugs that can modify or disrupt the intricate “dances” of proteins to alter their functions.
Dominique Frueh, PhD, associate professor of biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine, and colleagues, reported on their findings in Science Advances, in a paper titled “Global protein dynamics as communication sensors in peptide synthetase domains.” In their report, the team concluded “We demonstrated that structural fluctuations within a protein enable molecular discrimination by sensing post-translational modifications of binding partners to promote interactions accompanied by remodeling of distant sites.”
Proteins are organic compounds with blueprints that are found in DNA, and which function as the “business ends” of biology, making up the structural components of tissues, along with enzymes, which orchestrate chemical changes within cells.
It has long been known that proteins wiggle and move, but scientists have debated the significance of this “dancing” act, said Frueh. “The way proteins engage with the right partner at the right time—essentially, how they communicate—is very important for understanding their function,” he noted, “and we have found that protein wiggles are critical for this communication.”
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