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dc.contributor.authorDahanayake, Jayangika Niroshani
dc.contributor.authorKasireddy, Chandana
dc.contributor.authorEllis, Jonathan M.
dc.contributor.authorHildebrandt, Derek
dc.contributor.authorHull, Olivia A.
dc.contributor.authorKarnes, Joseph P.
dc.contributor.authorMorlan, Dylan
dc.contributor.authorMitchell-Koch, Katie R.
dc.identifier.citationJ. N. Dahanayake, C. Kasireddy, J. M. Ellis, D. Hildebrandt, O. A. Hull, J. P. Karnes, D. Morlan, K. R. Mitchell-Koch. J. Comput. Chem. 2017, 38, 2605–2617en_US
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractThe ability of electronic structure methods (11 density functionals, HF, and MP2 calculations; two basis sets and two solvation models) to accurately calculate the F-19 chemical shifts of 31 structures of fluorinated amino acids and analogues with known experimental F-19 NMR spectra has been evaluated. For this task, BHandHLYP, omega B97X, and HartreeFock with scaling factors (provided within) are most accurate. Additionally, the accuracy of methods to calculate relative changes in fluorine shielding across 23 sets of structural variants, such as zwitterionic amino acids versus side chains only, was also determined. This latter criterion may be a better indicator of reliable methods for the ultimate goal of assigning and interpreting chemical shifts of fluorinated amino acids in proteins. It was found that MP2 and M062X calculations most accurately assess changes in shielding among analogues. These results serve as a guide for computational developments to calculate F-19 chemical shifts in biomolecular environments.en_US
dc.description.sponsorshipNIH National Institute of General Medical Sciences (Wichita State University, Fairmount College of Liberal Arts and Sciences and K-INBRE); Contract grant number: P20 GM103418; Contract grant sponsor: National Science Foundation (State of Kansas and the Wichita State University High Performance Computing Center); Contract grant numbers: EIA-0216178 and EPS-0236913.en_US
dc.relation.ispartofseriesJournal of Computational Chemistry;v.38:no.30
dc.subjectFluorine NMRen_US
dc.subjectChemical shiftsen_US
dc.subjectFluorinated amino acidsen_US
dc.subjectDensity functionalen_US
dc.subjectScaling factorsen_US
dc.titleEvaluating electronic structure methods for accurate calculation of F-19 chemical shifts in fluorinated amino acidsen_US
dc.rights.holder(C) 2017 Wiley Periodicals, Inc.en_US

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