Residual chemical shift anisotropy explained

Residual chemical shift anisotropy (RCSA) is the difference between the chemical shift anisotropy (CSA) of aligned and non-aligned molecules. It is normally three orders of magnitude smaller than the static CSA, with values on the order of parts-per-billion (ppb). RCSA is useful for structural determination and it is among the new developments in NMR spectroscopy.

See also

• Residual dipolar coupling

Further reading

• Cornilescu . Gabriel . Bax . Ad . 2000 . Measurement of Proton, Nitrogen, and Carbonyl Chemical Shielding Anisotropies in a Protein Dissolved in a Dilute Liquid Crystalline Phase . Journal of the American Chemical Society . 122 . 41 . 10143–54 . 10.1021/ja0016194.
• Lipsitz . Rebecca S. . Tjandra . Nico . 2003 . 15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings . Journal of Magnetic Resonance . 164 . 1 . 171–6 . 2003JMagR.164..171L . 12932470 . 10.1016/S1090-7807(03)00176-9.
• Lipsitz . Rebecca S. . Tjandra . Nico . 2001 . Carbonyl CSA Restraints from Solution NMR for Protein Structure Refinement . Journal of the American Chemical Society . 123 . 44 . 11065–6 . 11686713 . 10.1021/ja016854g.
• Nath . Nilamoni . Schmidt . Manuel . Gil . Roberto R. . Wiliamson . R. Thomas . Martin . Gary E.. Navarro-Vázquez . Armando. Griesinger . Christian . Liu . Yhizhou . 2016 . Determination of Relative Configuration from Residual Chemical Shift Anisotropy . Journal of the American Chemical Society . 138 . 30 . 9548–56 . 27294984 . 10.1021/jacs.6b04082.