Scientists Crack Complex Enzyme Structure With Google's Help
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Scientists Crack Complex Enzyme Structure With Google’s Help

In a latest research study published in PNAS, a chemistry professor named Victor Batista & his fellow researchers at Yale have successfully identified key amino acids that regulate bacterial enzyme essential for almost all microorganisms with the use of Google’s PageRank algorithm. Via this novel approach, the researchers have cracked down the complex structure of enzymes & its regulation.

Enzymes have the unique property to accelerate chemical reactions. The substrates bind to the active site of the enzymes, where the reaction takes place. However, the acceleration or inhibition of a reaction takes place when a molecule binds to another site of the enzyme called the allosteric site. After decades of research, still, no proper information exists on how exactly the active site & the allosteric site of an enzyme communicate with each other. High flexible structurality of the enzyme & presence of an infinite number of atoms has made the identification process difficult.

Yale researchers noted that a similar question was addressed years before in the world of computer science. Researchers at Google had studied the flow of information online, using PageRank, an algorithm to signify the importance of each web page concerning the quantity and quality of links to

other Web websites.

Using the same PageRank, the team identified amino acids important for the allosteric process in imidazole glycerol phosphate synthase (IGPS), a bacterial enzyme found in most microorganisms.

This revolutionary research will set forth further experimentation & validation in this field keeping the current research outcome as a base. Advanced experimentation on IGPS activity may lead to the development of new antibiotics, pesticides, and herbicides.

This research was supported partially by National Institutes of Health and the National Science Foundation. The study’s other co-first author is Christian Negre of Los Alamos National Laboratory. Co-authors are Batista and J. Patrick Loria of Yale; former Yale researchers Heidi Hendrickson, Rhitankar Pal, and George Lisi; Ivan Rivalta of the University of Lyon; and Junming Ho of the University of New South Wales.

Courtesy: Yale news

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