Measurements of Proton Chemical Shift Anisotropy

Abstract

1H chemical shift anisotropy (CSA) measurements are useful for understanding molecule structure and dynamics. However, technically it remains a challenge due to strong 1H-1H homonuclear dipolar coupling interaction and relatively small 1H chemical shift anisotropy, especially in proteins with multiple proton sites. Here the current methods for 1H chemical shift anisotropy measurement are reviewed, including homonuclear decoupling slow magic angle spinning, ultrafast magic angle spinning, symmetry-based recoupling (RNnv) method, xCSA and quantum chemical calculations. Measurements of protein amide proton chemical shift anisotropy using solid state nuclear magnetic resonance (NMR) under fast magic angle spinning and correlations of amide proton chemical shift anisotropy with protein secondary structure/hydrogen bond length are discussed.

Keywords

• solid-state NMR
• review
• chemical shift anisotropy (CSA)
• proton
• hydrogen bond