Chemical shifts in amino acids, peptides, and proteins: From quantum chemistry to drug design

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Abstract

This chapter discusses recent progress in the investigation and use of 13C, 15N, and 19F 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.

Original languageEnglish (US)
Pages (from-to)349-378
Number of pages30
JournalAnnual Review of Physical Chemistry
Volume53
DOIs
StatePublished - 2002

Keywords

  • Electrostatics
  • Porphyrins

ASJC Scopus subject areas

  • Medicine(all)

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