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dc.contributor.authorKasireddy, Chandana
dc.contributor.authorEllis, Jonathan M.
dc.contributor.authorBann, James G.
dc.contributor.authorMitchell-Koch, Katie R.
dc.date.accessioned2017-03-14T23:19:53Z
dc.date.available2017-03-14T23:19:53Z
dc.date.issued2017-02-15
dc.identifier.citationKasireddy, Chandana; Ellis, Jonathan M.; Bann, James G.; Mitchell-Koch, Katie R. 2017. The biophysical probes 2-fluorohistidine and 4-fluorohistidine: spectroscopic signatures and molecular properties. Scientific Reports, vol. 7:article no. 42651en_US
dc.identifier.issn2045-2322
dc.identifier.otherWOS:000394252500001
dc.identifier.urihttp://dx.doi.org/10.1038/srep42651
dc.identifier.urihttp://hdl.handle.net/10057/12906
dc.descriptionThis work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material.en_US
dc.description.abstractFluorinated amino acids serve as valuable biological probes, by reporting on local protein structure and dynamics through F-19 NMR chemical shifts. 2-fluorohistidine and 4-fluorohistidine, studied here with DFT methods, have even more capabilities for biophysical studies, as their altered pK(a) values, relative to histidine, allow for studies of the role of proton transfer and tautomeric state in enzymatic mechanisms. Considering the two tautomeric forms of histidine, it was found that 2-fluorohistidine primarily forms the common (for histidine) t-tautomer at neutral pH, while 4-fluorohistidine exclusively forms the less common p-tautomer. This suggests the two isomers of fluorohistidine can also serve as probes of tautomeric form within biomolecules, both by monitoring NMR chemical shifts and by potential perturbation of the tautomeric equilibrium within biomolecules. Fluorine also enables assignment of tautomeric states in crystal structures. The differences in experimental pK(a) values between the isomers was found to arise from solvation effects, providing insight into the polarization and molecular properties of each isomer. Results also encompass C-13 and F-19 NMR chemical shifts, from both tautomers of 2-fluorohistidine and 4-fluorohistidine in a number of different environments. This work can serve as a guide for interpretation of spectroscopic results in biophysical studies employing 2-fluorohistidine and 4-fluorohistidine.en_US
dc.description.sponsorshipWichita State University, Fairmount College of Liberal Arts and Sciences and K-INBRE funds under NIH National Institute of General Medical Sciences, P20 GM103418. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of General Medical Sciences or the National Institutes of Health. Computing resources were funded by the National Science Foundation under Grant No. EIA-0216178 and Grant No. EPS-0236913, with matching support from the State of Kansas and the Wichita State University High Performance Computing Center.en_US
dc.language.isoen_USen_US
dc.publisherNature Publishing Groupen_US
dc.relation.ispartofseriesScientific Reports;v.7:article no. 42651
dc.subjectAnthrax protective antigenen_US
dc.subjectMagnetic-resonance-spectroscopyen_US
dc.subjectNMR chemical-shiftsen_US
dc.subjectColi dihydrofolate-reductaseen_US
dc.subjectHistidine-residuesen_US
dc.subjectTautomeric statesen_US
dc.subjectEscherichia-colien_US
dc.subjectF-19 NMRen_US
dc.subjectImidazole ringen_US
dc.subjectProtein structuresen_US
dc.titleThe biophysical probes 2-fluorohistidine and 4-fluorohistidine: spectroscopic signatures and molecular propertiesen_US
dc.typeArticleen_US
dc.rights.holder© 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved.en_US


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