| Synthetase polyspecificity as a tool to modulate protein function. | |
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MedLine Citation:
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PMID: 22041062 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The site-specific incorporation of unnatural amino acids (UAAs) into proteins in bacteria is made possible by the evolution of aminoacyl-tRNA synthetases that selectively recognize and aminoacylate the amino acid of interest. Recently we have discovered that some of the previously evolved aaRSs display a degree of polyspecificity and are capable of recognizing multiple UAAs. Herein we report the polyspecificity of an aaRS evolved to encode a comarin containing amino acid. This polyspecificity was then exploited to introduce several UAAs into the fluorophore of GFP, altering its photophysical properties. |
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Authors:
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Douglas D Young; Steffen Jockush; Nicholas J Turro; Peter G Schultz |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-8 |
Journal Detail:
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Title: Bioorganic & medicinal chemistry letters Volume: - ISSN: 1464-3405 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-11-1 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9107377 Medline TA: Bioorg Med Chem Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, United States. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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