3S-fluoroproline as a probe to monitor proline isomerization during protein folding by 19F-NMR

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dc.contributor Wichita State University. Department of Chemistry en_US
dc.contributor.author Thomas, Colin A. en_US
dc.contributor.author Talaty, Erach R. en_US
dc.contributor.author Bann, James G. en_US
dc.date.accessioned 2012-02-06T17:16:09Z
dc.date.available 2012-02-06T17:16:09Z
dc.date.issued 2009-06-21 en_US
dc.identifier 19503872 en_US
dc.identifier 9610838 en_US
dc.identifier.citation Chemical communications (Cambridge, England). 2009 Jun 21; (23): 3366-8. en_US
dc.identifier.issn 1359-7345 en_US
dc.identifier.uri http://dx.doi.org/10.1039/b821952d en_US
dc.identifier.uri http://hdl.handle.net/10057/4312
dc.description Click on the DOI link below to access the article (may not be free). en_US
dc.description.abstract Variable-temperature inversion transfer NMR is used to determine the kinetic and thermodynamic parameters of cis-trans isomerization of N-Ac-(3R) and (3S)-fluoroproline-OMe. en_US
dc.format.extent 3366-8 en_US
dc.language.iso eng en_US
dc.publisher Royal Society of Chemistry en_US
dc.relation.ispartofseries Chemical communications (Cambridge, England) en_US
dc.relation.ispartofseries Chem. Commun. (Camb.) en_US
dc.source NLM en_US
dc.subject Research Support, N.I.H., Extramural en_US
dc.subject Research Support, Non-U.S. Gov't en_US
dc.subject.mesh Deuterium Oxide/chemistry en_US
dc.subject.mesh Kinetics en_US
dc.subject.mesh Magnetic Resonance Spectroscopy en_US
dc.subject.mesh Proline/analogs & derivatives en_US
dc.subject.mesh Protein Folding en_US
dc.subject.mesh Stereoisomerism en_US
dc.subject.mesh Thermodynamics en_US
dc.subject.mesh Proline/chemistry en_US
dc.title 3S-fluoroproline as a probe to monitor proline isomerization during protein folding by 19F-NMR en_US
dc.type Article en_US
dc.coverage.spacial England en_US
dc.description.version peer reviewed en_US
dc.rights.holder Copyright © 2009, Royal Society of Chemistry en_US

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