Chemical-shift ranges in proteins

Joseph Augspurger, John G. Pearson, Eric Oldfield, Clifford E. Dykstra, Ki Deok Park, Dwight Schwartz

Research output: Contribution to journalArticlepeer-review

Abstract

The results of ab initio derivative Hartree-Fock calculations of the dipole and quadrupole shielding polarizabilities and hyperpolarizabilities of a number of small molecules are reported, together with estimates of the electric fields and field gradients present in proteins. It is argued that weak electrical interactions, mediated via these shielding polarizabilities, make major contributions to the chemical-shift nonequivalencies observed in proteins due to folding into their native conformations. The electric-field-induced shifts may be very large (≈5 ppm for 13C, ≈10 ppm for 17O and 17F), due to the low dielectric constants found in proteins, and in some cases they may dominate the experimentally observed spectral shifts.

Original languageEnglish (US)
Pages (from-to)342-357
Number of pages16
JournalJournal of Magnetic Resonance (1969)
Volume100
Issue number2
DOIs
StatePublished - Nov 1992

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