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109283 |
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|a Vinogradov, Alexander Alexandrovich
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|a Massachusetts Institute of Technology. Department of Chemistry
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|a Vinogradov, Alexander Alexandrovich
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|a Evans, Ethan Daniel
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|a Pentelute, Bradley L.
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|a Evans, Ethan Daniel
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|a Pentelute, Bradley L.
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|a Total synthesis and biochemical characterization of mirror image barnase
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|b Royal Society of Chemistry, The,
|c 2017-05-23T13:58:16Z.
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|z Get fulltext
|u http://hdl.handle.net/1721.1/109283
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|a In this study we synthesized and characterized mirror image barnase (B. amyloliquefaciens ribonuclease). D-Barnase was identical to L-barnase, when analyzed by liquid chromatography and mass-spectrometry. Proteolysis of the mirror image enzyme revealed that in contrast to its native counterpart, D-barnase was completely stable to digestive proteases. In enzymatic assays, D-barnase had the reciprocal chiral specificity and was fully active towards mirror image substrates. Interestingly, D-barnase also hydrolyzed the substrate of the native chirality, albeit 4000 times less efficiently. This effect was further confirmed by digesting a native 112-mer RNA with the enzyme. Additional studies revealed that barnase accommodates a range of substrates with various chiralities, but the prime requirement for guanosine remains. These studies point toward using mirror image enzymes as modern agents in biotechnology.
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|a United States. Defense Advanced Research Projects Agency (023504-001)
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|a en_US
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|a Article
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|t Chemical Science
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