Johns Hopkins Medicine scientists report they have probed the atomic structure of proteins to add to evidence that the wobbles, shakes and quivers of proteins play a critical role in their ability to function. The findings of the research may help scientists design new drugs that can modify or disrupt the intricate “dances” of proteins to alter their functions.
Results of the researchers’ experiments will be published in the July 15 issue of Science Advances.
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.
Though it has long been known that proteins wiggle and move, scientists have debated the significance of this “dancing” act, says Dominique Frueh, Ph.D., associate professor of biophysics and biophysical chemistry at the Johns Hopkins University School of Medicine. “The way proteins engage with the right partner at the right time — essentially, how they communicate — is very important for understanding their function,” he says, “and we have found that protein wiggles are critical for this communication.”
In a bid to further such understanding, Frueh’s team studied the wiggling action of the HMWP2 protein, a type of enzyme called nonribosomal peptide synthetases. These enzymes are made of several domains, or distinct regions, that work together like an assembly line to make complex natural products from small chemicals.
These natural products often have pharmaceutical properties, such as bacitracin, found in topical antibiotic ointments. In the case of HMWP2, its product is yersiniabactin, a molecule that scavenges iron molecules for bacteria, including Escherichia coli, found in urinary tract infections, and Yersinia pestis, the bacterium that causes bubonic plague.
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