Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach

Angel C. De Dios, John G. Pearson, Eric Oldfield

Research output: Contribution to journalArticlepeer-review

Abstract

Recent theoretical developments permit the prediction of 1H, 13C, 15N, and 19F nuclear magnetic resonance chemical shifts in proteins and offer new ways of analyzing secondary and tertiary structure as well as for probing protein electrostatics. For 13C, φ,Ψ torsion angles dominate shielding for Cα and Cβ, but the addition of hydrogen bonding and electrostatics gives even better accord with experiment For 15NH, side chain (χ1) torsion angles are also important, as are nearest neighbor sequence effects, whereas for 1HN, hydrogen bonding is particularly significant For 19F, weak or long-range electrostatic fields dominate 19F shielding nonequivalencies. The ability to predict chemical shifts in proteins from known or test structures opens new avenues to structure refinement or determination, especially for condensed systems.

Original languageEnglish (US)
Pages (from-to)1491-1496
Number of pages6
JournalScience
Volume260
Issue number5113
StatePublished - 1993

ASJC Scopus subject areas

  • General

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