Structural information from NMR secondary chemical shifts of peptide α C-H protons in proteins

Abstract

The secondary chemical shift experienced by the 1H-NMR resonances of the alpha C-H protons in proteins can be correlated with their backbone torsional angles psi, which dictate the orientation of the alpha C-H proton to the adjacent carbonyl group. It is shown that alpha C-H protons present in beta-sheet regions experience downfield secondary shifts, whereas those in alpha-helix regions experience upfield secondary shifts. The predictive use of this correlation in assignment studies is illustrated for the calcium-binding protein paravalbumin, for which a crystal structure is available, and troponin C, for which no crystallographic data are available.