A strange protein structure known as an “undulated beta sheet,” first anticipated in quite a while, has been made in the lab and portrayed exhaustively utilizing X-beam crystallography.
The new discoveries, published in July in Chemical Science, may enhance the sane design of novel materials in view of the undulated sheet design.
“Our review lays out the undulated beta sheet layer setup as a theme with general elements and opens the door to structure-based planning of novel sub-atomic models, with potential for materials improvement and biomedical applications,” said Jevgenij Raskatov, academic partner of science and organic chemistry at UC Santa Cruz and the paper’s creator.
Proteins arrive in a huge variety of shapes and sizes to do their incredibly primary and useful jobs in living cells. Certain normal primary themes, like the alpha helix, are found in numerous protein structures.
“Our research establishes the rippling beta sheet layer arrangement as a motif with generic properties and paves the way for structure-based design of unique molecular architectures with promise for materials development and biological applications.”
Jevgenij Raskatov, associate professor of chemistry
The undulated sheet is a minor departure from the creased beta sheet, a notable primary theme tracked down in a great many proteins. Two years after presenting the idea of the creased beta sheet, Linus Pauling and Robert Corey depicted the undulated beta sheet in 1953. While the creased beta sheet is notable and frequently called just the beta sheet, the undulated sheet stayed a generally hypothetical design for quite a long time.
In a past report distributed in Chemical Science in 2021, Raskatov’s group revealed getting an undulated beta sheet structure by blending a little peptide in with equivalent measures of its perfect representation. The scientists utilized perfect representation types of triphenylalanine, a short peptide comprised of three phenylalanine amino acids. The perfect representation peptides participated two by two to shape “dimers” with the anticipated design, yet they didn’t frame the lengthy, occasional undulated beta-sheet layer geology guessed by Pauling and Corey.
“The dimers pressed together into herringbone layer structures, which raised uncertainty regarding whether the occasional undulated beta-sheet layer setup was suitable,” Raskatov said.
In the new review, the analysts subbed other amino acids for one of the triphenylalanines to make somewhat unique tripeptides and their perfect representations. Utilizing these new tripeptides, they had the option to make three different amassing peptide frameworks that shaped expanded antiparallel undulated beta sheet layers, in which perfect representation peptide strands were organized in a rotating style. The consequences of X-beam crystallography showed that the gem structures are in great general concurrence with the forecasts made by Pauling and Corey.
More information: Amaruka Hazari et al, The rippled β-sheet layer configuration—a novel supramolecular architecture based on predictions by Pauling and Corey, Chemical Science (2022). DOI: 10.1039/d2sc02531k
Ariel J. Kuhn et al, A crystal-structural study of Pauling–Corey rippled sheets, Chemical Science (2021). DOI: 10.1039/D1SC05731F
Journal information: Chemical Science
