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• W2021984952 abstract "Abstract The introduction of non‐natural modules could provide unprecedented control over folding/unfolding behavior, conformational stability, and biological function of proteins. Success requires the interrogation of candidate modules in natural contexts. Here, expressed protein ligation is used to replace a reverse turn in bovine pancreatic ribonuclease (RNase A) with a synthetic β‐dipeptide: β 2 ‐homoalanine–β 3 ‐homoalanine. This segment is known to adopt an unnatural reverse‐turn conformation that contains a 10‐membered ring hydrogen bond, but one with a donor–acceptor pattern opposite to that in the 10‐membered rings of natural reverse turns. The RNase A variant has intact enzymatic activity, but unfolds more quickly and has diminished conformational stability relative to native RNase A. These data indicate that hydrogen‐bonding pattern merits careful consideration in the selection of beneficial reverse‐turn surrogates." @default.
• W2021984952 created "2016-06-24" @default.
• W2021984952 creator A5004872881 @default.
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• W2021984952 date "2013-01-17" @default.
• W2021984952 modified "2023-10-18" @default.
• W2021984952 title "Protein prosthesis: β-peptides as reverse-turn surrogates" @default.
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• W2021984952 doi "https://doi.org/10.1002/pro.2208" @default.
• W2021984952 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3595457" @default.
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