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- W2033680332 abstract "ψ[CS−NH]4-RNase S, a site specific modified version of RNase S obtained by thioxylation (O/S exchange) at the Ala4-Ala5- peptide bond, was used to evaluate the impact of protein backbone photoswitching on bioactivity. ψ[CS−NH]4-RNase S was yielded by recombination of the S-protein and the respective chemically synthesized thioxylated S-peptide derivative. Comparison with RNase S revealed similar thermodynamic stability of the complex and an unperturbed enzymatic activity toward cytidine 2‘,3‘-cyclic monophosphate (cCMP). Reversible photoisomerization with a highly increased cis/trans isomer ratio of the thioxopeptide bond of ψ[CS−NH]4-RNase S in the photostationary state occurred under UV irradiation conditions (254 nm). The slow thermal reisomerization (t1/2 = 180 s) permitted us to determine the enzymatic activity of cis ψ[CS−NH]4-RNase S by measurement of inital rates of cCMP hydrolysis. Despite thermodynamic stability of cis ψ[CS−NH]4-RNase S, its enzymatic activity is completely abolished but recovers after reisomerization. We conclude that the thioxopeptide bond modified polypeptide backbone represents a versatile probe for site-directed photoswitching of proteins." @default.
- W2033680332 created "2016-06-24" @default.
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- W2033680332 date "2007-03-31" @default.
- W2033680332 modified "2023-10-18" @default.
- W2033680332 title "A Nearly Isosteric Photosensitive Amide-Backbone Substitution Allows Enzyme Activity Switching in Ribonuclease S" @default.
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- W2033680332 doi "https://doi.org/10.1021/ja069048o" @default.
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