A new study offers new insights into the evolution of foldable proteins.
A new study led by Rice University's Peter Wolynes offers new insights into the evolution of foldable proteins. The research was published in theResearchers at Rice and the University of Buenos Aires used energy landscape theory to distinguish between foldable and nonfoldable parts of protein sequences. Their study illuminates the ongoing debate about whether the pieces of DNA that code for only part of a protein during their origins can fold on their own.
When genes in pieces were discovered in the 1970s, it was immediately proposed that by breaking up the sequence, this structure helped build foldable proteins. When researchers looked at this again in the 1990s, the existing data was equivocal, Wolynes said. Natural proteins are linear chains of amino acids that typically fold into compact three-dimensional structures to perform biological functions. The specific sequence of amino acids dictates the final 3D structure. Therefore, the idea that exons translate into independently folded protein regions, or foldons, is very attractive.
Interestingly, the general trend did not hold for all protein families, suggesting that other biological factors may influence protein folding and evolution. The researchers' work paves the way for future studies to understand these additional factors and their impact on evolutionary biology.A new study brings together intriguing details about the little-known Rhabdodontidae dinosaurs of Late Cretaceous Europe. These gregarious herbivores, characterized by robust builds and beaks ...
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