Computing nuclear magnetic resonance chemical shielding in large systems via multipole shielding polarizabilities

Augspurger, Joseph D.; DeDios, Angel C.; Oldfield, Eric; Dykstra, Clifford E.

doi:10.1016/0009-2614(93)85122-5

Cited by 19 publications

(25 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These shielding polarizability tensor elements, when multiplied by the appropriate field, field gradient, or hypergradient terms (which can be readily calculated from the known charge distributions, at least in the H-F molecule), yield the electrical contributions to shielding. A comparison of the multipole shielding polarizability expansion truncated at the point of linear field, field gradient, and hypergradient terms was found to be in excellent accord with benchmark ab initio results, both for a dipole and for a point-charge perturbation (54). On this basis, we concluded that super-molecule, point charge, and low-order MSP expansions permitted the accurate determination of the electrical contributions to shielding in model systems and should therefore be applicable to proteins as well.…”

Section: Fluorine-19 Nmr and Electrostatic Field Effectssupporting

confidence: 67%

“…We then used a second approach, which involved determining the multipole shielding polarizabilities (MSP) of fluorobenzene: how the tensor elements change with electrical polarization (54). Dykstra used derivative Hartree-Fock methods to calculate the MSP tensor elements for the 19 F nucleus in fluorobenzene with respect to a uniform field, a field gradient, and a field-hypergradient.…”

Section: Fluorine-19 Nmr and Electrostatic Field Effectsmentioning

confidence: 99%

See 1 more Smart Citation

CHEMICALSHIFTS INAMINOACIDS, PEPTIDES,ANDPROTEINS: From Quantum Chemistry to Drug Design

Oldfield

2002

Annu. Rev. Phys. Chem.

Self Cite

117

View full text Add to dashboard Cite

This chapter discusses recent progress in the investigation and use of (13)C, (15)N, and (19)F nuclear magnetic resonance (NMR) chemical shifts and chemical shift tensors in proteins and model systems primarily using quantum chemical (ab initio Hartree-Fock and density functional theory) techniques. Correlations between spectra and structure are made and the techniques applied to other spectroscopic and electrostatic properties as well, including hydrogen bonding, ligand binding to heme proteins, J-couplings, electric field gradients, and atoms-in-molecules theory, together with a brief review of the use of NMR chemical shifts in drug design.

show abstract

Section: Fluorine-19 Nmr and Electrostatic Field Effectssupporting

confidence: 67%

Section: Fluorine-19 Nmr and Electrostatic Field Effectsmentioning

confidence: 99%

CHEMICALSHIFTS INAMINOACIDS, PEPTIDES,ANDPROTEINS: From Quantum Chemistry to Drug Design

Oldfield

2002

Annu. Rev. Phys. Chem.

Self Cite

117

View full text Add to dashboard Cite

show abstract

“…The use of a uniform electric field hinges on the adequacy of truncating the Taylor series expansion of the chemical shift with respect to a nonuniform electric field at the first term. Previous work has shown that terms arising from the field gradient and the hypergradient are also significant . It should also be noted that the contribution from the field gradient is opposite in sign to that of the uniform field.…”

Section: Resultsmentioning

confidence: 93%

Electric Field Effects on ¹³C and ¹⁷O Chemical Shifts and CO Stretching Frequency of Carbon Monoxide Bound to Fe²⁺

Dios

Earle

1997

J. Phys. Chem. A

View full text Add to dashboard Cite

Using a model consisting of Fe2+ octahedrally coordinated to five negative point charges and a CO molecule, the effects of a uniform external electric field applied along the Fe−C−O axis on the chemical shifts of 13C and 17O and the CO stretching frequency are investigated. Both the vibrational frequency and the 17O chemical shift are observed to increase as the electric field applied parallel to the Fe−C−O axis is increased. On the other hand, the 13C chemical shift changes in the opposite direction. The influence of a nonuniform field is also studied by introducing an additional variable point charge along the Fe−C−O axis. Results of the calculations agree well with observed correlations of 13C and 17O chemical shifts and CO vibrational frequencies in carbonmonoxy heme proteins.

show abstract

“…Hyperpolarizabilities (v 2 /vF 2 ) and mixed derivatives (v 2 /vF vV ) were also evaluated (Augspurger et al 1993b), but based on the results of model calculations, only theÃ andB tensors were found to be significant. The results of these 'multipole shielding polarizability' calculations on the fluorobenzene-HF clusters were found to agree with those obtained from supermolecule or CFP techniques (Augspurger et al 1993b;. What this means for proteins is that the electrostatic contributions to the 19 F NMR chemical shifts can be calculated by simply multiplying theÃ andB tensors by the electrostatic fields and field gradients in the protein.…”

Section: Fluorine Nmr Chemical Shifts and Electrostaticsmentioning

confidence: 99%

“…That is,Ã is the formal derivative of s with respect to a uniform field, whileB is the formal derivative of s with respect to the non-uniform field or field gradient components. Hyperpolarizabilities (v 2 /vF 2 ) and mixed derivatives (v 2 /vF vV ) were also evaluated (Augspurger et al 1993b), but based on the results of model calculations, only theÃ andB tensors were found to be significant. The results of these 'multipole shielding polarizability' calculations on the fluorobenzene-HF clusters were found to agree with those obtained from supermolecule or CFP techniques (Augspurger et al 1993b;.…”

Section: Fluorine Nmr Chemical Shifts and Electrostaticsmentioning

confidence: 99%

Quantum chemical studies of protein structure

Oldfield

2004

Phil. Trans. R. Soc. B

Self Cite

View full text Add to dashboard Cite

Quantum chemical methods now permit the prediction of many spectroscopic observables in proteins and related model systems, in addition to electrostatic properties, which are found to be in excellent accord with those determined from experiment. I discuss the developments over the past decade in these areas, including predictions of nuclear magnetic resonance chemical shifts, chemical shielding tensors, scalar couplings and hyperfine (contact) shifts, the isomer shifts and quadrupole splittings in Mö ssbauer spectroscopy, molecular energies and conformations, as well as a range of electrostatic properties, such as charge densities, the curvatures, Laplacians and Hessians of the charge density, electrostatic potentials, electric field gradients and electrostatic field effects. The availability of structure/spectroscopic correlations from quantum chemistry provides a basis for using numerous spectroscopic observables in determining aspects of protein structure, in determining electrostatic properties which are not readily accessible from experiment, as well as giving additional confidence in the use of these techniques to investigate questions about chemical bonding and chemical reactions.

show abstract

Computing nuclear magnetic resonance chemical shielding in large systems via multipole shielding polarizabilities

Cited by 19 publications

References 31 publications

CHEMICALSHIFTS INAMINOACIDS, PEPTIDES,ANDPROTEINS: From Quantum Chemistry to Drug Design

CHEMICALSHIFTS INAMINOACIDS, PEPTIDES,ANDPROTEINS: From Quantum Chemistry to Drug Design

Electric Field Effects on ¹³C and ¹⁷O Chemical Shifts and CO Stretching Frequency of Carbon Monoxide Bound to Fe²⁺

Quantum chemical studies of protein structure

Contact Info

Product

Resources

About

Computing nuclear magnetic resonance chemical shielding in large systems via multipole shielding polarizabilities

Cited by 19 publications

References 31 publications

CHEMICALSHIFTS INAMINOACIDS, PEPTIDES,ANDPROTEINS: From Quantum Chemistry to Drug Design

CHEMICALSHIFTS INAMINOACIDS, PEPTIDES,ANDPROTEINS: From Quantum Chemistry to Drug Design

Electric Field Effects on 13C and 17O Chemical Shifts and CO Stretching Frequency of Carbon Monoxide Bound to Fe2+

Quantum chemical studies of protein structure

Contact Info

Product

Resources

About

Electric Field Effects on ¹³C and ¹⁷O Chemical Shifts and CO Stretching Frequency of Carbon Monoxide Bound to Fe²⁺