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dc.contributor.authorKrueger, Andrew T.
dc.contributor.authorImperiali, Barbara
dc.date.accessioned2014-04-03T13:46:07Z
dc.date.available2014-04-03T13:46:07Z
dc.date.issued2013-04
dc.date.submitted2013-02
dc.identifier.issn14394227
dc.identifier.issn1439-7633
dc.identifier.urihttp://hdl.handle.net/1721.1/85981
dc.description.abstractFluorescence spectroscopy is a powerful tool for probing complex biological processes. The ubiquity of peptide–protein and protein–protein interactions in these processes has made them important targets for fluorescence labeling, and to allow sensitive readout of information concerning location, interactions with other biomolecules, and macromolecular dynamics. This review describes recent advances in design, properties and applications in the area of fluorescent amino acids (FlAAs). The ability to site-selectively incorporate fluorescent amino acid building blocks into a protein or peptide of interest provides the advantage of closely retaining native function and appearance. The development of an array of fluorescent amino acids with a variety of properties, such as environment sensitivity, chelation-enhanced fluorescence, and profluorescence, has allowed researchers to gain insights into biological processes, including protein conformational changes, binding events, enzyme activities, and protein trafficking and localization.en_US
dc.language.isoen_US
dc.publisherWiley Blackwellen_US
dc.relation.isversionofhttp://dx.doi.org/10.1002/cbic.201300079en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alikeen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/en_US
dc.sourceImperiali via Courtney Crummetten_US
dc.titleFluorescent Amino Acids: Modular Building Blocks for the Assembly of New Tools for Chemical Biologyen_US
dc.typeArticleen_US
dc.identifier.citationKrueger, Andrew T., and Barbara Imperiali. “Fluorescent Amino Acids: Modular Building Blocks for the Assembly of New Tools for Chemical Biology.” ChemBioChem 14, no. 7 (May 10, 2013): 788–799.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.approverImperiali, Barbaraen_US
dc.contributor.mitauthorKrueger, Andrew T.en_US
dc.contributor.mitauthorImperiali, Barbaraen_US
dc.relation.journalChemBioChemen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsKrueger, Andrew T.; Imperiali, Barbaraen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-5749-7869
mit.licenseOPEN_ACCESS_POLICYen_US
mit.metadata.statusComplete


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