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01701 am a22003253u 4500 |
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95629 |
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|a dc
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|a Zhang, Chi
|e author
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|a Massachusetts Institute of Technology. Department of Chemistry
|e contributor
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|a Zhang, Chi
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|a Spokoyny, Alexander M.
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|a Zou, Yekui
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|a Simon, Mark
|e contributor
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|a Pentelute, Bradley L.
|e contributor
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|a Spokoyny, Alexander M.
|e author
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|a Zou, Yekui
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|a Pentelute, Bradley L.
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|a Simon, Mark
|e author
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|a Enzymatic "Click" Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
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|b Wiley Blackwell,
|c 2015-02-25T20:15:29Z.
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|z Get fulltext
|u http://hdl.handle.net/1721.1/95629
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|a Singled out for special treatment: Naturally occurring glutathione S-transferase (GST) was used to catalyze an efficient "click" ligation between polypeptides with an N-terminal glutathione sequence and biomolecules or chemical probes containing perfluorinated aromatic groups (see scheme). The site-specific modification of one cysteine residue was possible in the presence of other unprotected cysteine residues and reactive functional groups.
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|a National Institutes of Health (U.S.) (GM101762)
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|a National Institutes of Health (U.S.) (Award GM46059)
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|a MIT Faculty Start-up Fund
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|a Damon Runyon Cancer Research Foundation
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|a Amgen Inc. (Summer Graduate Research Fellowship)
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|a en_US
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|a Article
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|t Angewandte Chemie International Edition
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