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Figure: Ripple betas are variants of ruffled betas, a well-known structural motif found in thousands of proteins
Image credit: J.
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 the journal Chemical Science in July, may enable the rational design of unique materials based on corrugated sheet-like structures
"Our study establishes the corrugated beta sheet configuration as a universally characterized motif, and as a unique structure-based Molecular structure design opens the way, with 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
The corrugated sheet is a variation of β sheet, a well-known structural motif found in thousands of proteins
In a previous study published in 2021, Raskatov's team reported that by mixing small peptides with an equal amount of mirror images, they obtained corrugated beta sheet structures
"The dimers clustered together to form a chevron-shaped layer structure, which raised doubts about whether a periodically corrugated beta-sheet structure was feasible," Raskatov said
In the new study, the researchers replaced one of the triphenylalanines with other amino acids, resulting in a slightly different tripeptide and its mirror image
One of the first authors of the paper is Raskatov's lab staff members Amaruka Hazari and UCLA's Michael Sawaya
