NMR and quantum chemistry of proteins and model systems

Christina M. Szabo; Lori K. Sanders; William Arnold; Joshua S. Grimley; Nathalie Godbout; Michael T. McMahon; Benjamin Moreno; Eric Oldfield

doi:10.1021/bk-1999-0732.ch003

NMR and quantum chemistry of proteins and model systems

Christina M. Szabo, Lori K. Sanders, William Arnold, Joshua S. Grimley, Nathalie Godbout, Michael T. McMahon, Benjamin Moreno, Eric Oldfield

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

We report the results of experimental and theoretical studies of ¹³C and ¹⁵N shifts in proteins and model systems, together with ⁵⁷Fe shifts and Mössbauer quadrupole splittings (electric field gradients) in metalloporphyrins and metalloproteins. The ability to relate these spectroscopic observables to structure by using quantum chemical methods opens up new opportunities for predicting and refining protein structure.

Original language	English (US)
Pages (from-to)	40-62
Number of pages	23
Journal	ACS Symposium Series
Volume	732
DOIs	https://doi.org/10.1021/bk-1999-0732.ch003
State	Published - 1999

ASJC Scopus subject areas

General Chemistry
General Chemical Engineering

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10.1021/bk-1999-0732.ch003

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author = "Szabo, {Christina M.} and Sanders, {Lori K.} and William Arnold and Grimley, {Joshua S.} and Nathalie Godbout and McMahon, {Michael T.} and Benjamin Moreno and Eric Oldfield",

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AU - Szabo, Christina M.

AU - Sanders, Lori K.

AU - Arnold, William

AU - Grimley, Joshua S.

AU - Godbout, Nathalie

AU - McMahon, Michael T.

AU - Moreno, Benjamin

AU - Oldfield, Eric

PY - 1999

Y1 - 1999

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AB - We report the results of experimental and theoretical studies of 13C and 15N shifts in proteins and model systems, together with 57Fe shifts and Mössbauer quadrupole splittings (electric field gradients) in metalloporphyrins and metalloproteins. The ability to relate these spectroscopic observables to structure by using quantum chemical methods opens up new opportunities for predicting and refining protein structure.

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NMR and quantum chemistry of proteins and model systems

Abstract

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