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• W2024889502 abstract "Disulfide bonds play fundamental roles in proteins. This work is devoted to highly rare motifs containing disulfide bonds. A search for four cysteines, forming a 16-atom membered ring (4CR) embodying two disulfide bonds, was carried out against all entries in the Protein Data Bank. Searching the crystallographic subset, only few protein molecules, all dimeric, were found to embody this peculiar structural feature, which establishes a covalent link between two different polypeptide chains. In contrast, in a peptide studied in solution by NMR, the four cysteines moiety includes only residues from one chain. A comparative analysis provided evidence for similarity and difference. It emerged that 4CR motif is highly rare and may serve to gain a specialized function. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1048–1055, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]" @default.
• W2024889502 created "2016-06-24" @default.
• W2024889502 creator A5054854944 @default.
• W2024889502 date "2009-12-01" @default.
• W2024889502 modified "2023-09-25" @default.
• W2024889502 title "The four cysteines ring motif in proteins" @default.
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• W2024889502 doi "https://doi.org/10.1002/bip.21280" @default.
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