The rippled beta sheet is a variation of the pleated beta sheet, a well known structural motif present in hundreds of proteins. Linus Pauling and Robert Corey described the rippled beta sheet in 1953, but it surely remained a largely theoretical construction for many years. Scientists have now created rippled sheets within the laboratory and characterised the construction utilizing x-ray crystallography. Credit: J. Raskatov
University of California, Santa Cruz, scientists report the creation of three crystal constructions of periodic rippled beta sheets, a novel protein construction.
A peculiar protein construction generally known as a “rippled beta sheet,” which was initially hypothesized in 1953, has now been generated within the laboratory and completely characterised utilizing x-ray crystallography.
The new findings, which have been revealed within the journal Chemical Science, might enable for the rational design of distinctive supplies primarily based on the rippled sheet structure.
“Our study establishes the rippled beta sheet layer configuration as a motif with general features and opens the road to the structure-based design of unique molecular architectures, with potential for materials development and biomedical applications,” mentioned Jevgenij Raskatov, affiliate professor of chemistry and biochemistry on the University of California, Santa Cruz and corresponding writer of the paper.
Proteins exist in a variety of sizes and styles to satisfy their many structural and practical roles in residing cells. Many protein constructions have frequent structural motifs, such because the alpha helix.
The rippling sheet is a variant of the pleated beta sheet, a well known structural motif current in hundreds of proteins. Linus Pauling and Robert Corey described the rippled beta sheet two years after introducing the pleated beta sheet idea. While the pleated beta sheet is usually identified and generally referred to easily because the beta sheet, the rippled sheet has remained theoretical for many years.
In a earlier research revealed in 2021, Raskatov’s crew reported acquiring a rippled beta sheet construction by mixing a small peptide with equal quantities of its mirror picture. The researchers used mirror-image types of triphenylalanine, a brief peptide consisting of three phenylalanine amino acids. The mirror-image peptides joined in pairs to form “dimers” with the predicted structure, but they did not form the extended, periodic rippled beta-sheet layer topography hypothesized by Pauling and Corey.
“The dimers packed together into herringbone layer structures, which raised doubt as to whether the periodic rippled beta-sheet layer configuration was viable,” Raskatov said.
In the new study, the researchers substituted other amino acids for one of the triphenylalanines to create slightly different tripeptides and their mirror images. Using these new tripeptides, they were able to create three different aggregating peptide systems that formed extended antiparallel rippled beta sheet layers, in which mirror-image peptide strands were arranged in an alternating fashion. The results of x-ray crystallography showed that the crystal structures are in excellent overall agreement with the predictions made by Pauling and Corey.
Reference: “The rippled β-sheet layer configuration—a novel supramolecular architecture based on predictions by Pauling and Corey” by Amaruka Hazari, Michael R. Sawaya, Niko Vlahakis, Timothy C. Johnstone, David Boyer, Jose Rodriguez, David Eisenberg and Jevgenij A. Raskatov, 15 July 2022, Chemical Science.
DOI: 10.1039/d2sc02531k
