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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
References
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. Bibcode:2000JAChS.12210143C. doi: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. Bibcode:2003JMagR.164..171L. doi:10.1016/S1090-7807(03)00176-9. PMID 12932470.
- 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. Bibcode:2001JAChS.12311065L. doi:10.1021/ja016854g. PMID 11686713.
- 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. Bibcode:2016JAChS.138.9548N. doi:10.1021/jacs.6b04082. PMID 27294984.
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