Calculation of chemical shift anisotropy in proteins

Sishi Tang, David A. Case

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

Individual peptide groups in proteins must exhibit some variation in the chemical shift anisotropy (CSA) of their constituent atoms, but not much is known about the extent or origins of this dispersion. Direct spectroscopic measurement of CSA remains technically challenging, and theoretical methods can help to overcome these limitations by estimating shielding tensors for arbitrary structures. Here we use an automated fragmentation quantum mechanics/molecular mechanics (AF-QM/MM) approach to compute 15N, 13C′ and 1H chemical shift tensors for human ubiquitin and the GB1 and GB3 fragments of staphylococcal protein G. The average and range of variation of the anisotropies is in good agreement with experimental estimates from solid-state NMR, and the variation among residues is somewhat smaller than that estimated from solution-state measurements. Hydrogen-bond effects account for much of the variation, both between helix and sheet regions, and within elements of secondary structure, but other effects (including variations in torsion angles) may play a role as well.

Original languageEnglish (US)
Pages (from-to)303-312
Number of pages10
JournalJournal of biomolecular NMR
Volume51
Issue number3
DOIs
StatePublished - Nov 2011

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Spectroscopy

Keywords

  • Anisotropy
  • Chemical shift
  • Proteins

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