An unusual protein structure called a “corrugated beta sheet”, first predicted in 1953, has now been created in the laboratory and characterized in detail using X-ray crystallography.
The new findings, published in Chemical Science in July, may enable the rational design of unique materials based on corrugated sheet-like structures.
Jevgenij Raskatov, associate professor of chemistry and biochemistry at the University of California, Santa Cruz and corresponding author of the paper, said: “Our study establishes the corrugated beta sheet configuration as a motif with universal characteristics, and opens the way for structure-based design of unique molecular structures with the potential for material development and biomedical applications.”
Proteins come in ever-changing shapes and sizes and play a wide variety of structural and functional roles in living cells. Certain common structural motifs, such as alpha helices, are found in many protein structures.
Corrugated sheet is a variation of β sheet, which is a famous structural motif found in thousands of proteins. Linus Pauling and Robert Corey described corrugated beta flakes in 1953, and two years ago they proposed the concept of corrugated beta flakes. Although the folded beta sheet corrugated beta sheet is well-known and often simple called beta sheet,corrugated beta sheets have remained largely a theoretical structure for decades.
The x-ray crystallography results showed that the crystal structure was basically consistent with Pauling and Corey’s predictions.
One of the paper’s first author is Raskatov’s lab staff Amaruka Hazari and UCLA’s Micheal Sawaya. Other co-authors include Timothy Johnstone of UC Santa Cruz and Niko Vlahakis,David Boyer of UCLA. This researchers was supported by the National Institution of Health.
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