Phosphorus-31 NMR as a probe for phosphoproteins.

Abstract

Nuclear magnetic resonance methodology continues to advance such that phosphorus-31 NMR experiments can be profitably applied to elucidate some aspects of proteins which are covalently phosphorylated. This review introduces NMR spectral parameters pertinent to using phosphorus-31 NMR for investigation of structure and dynamics. The techniques of two-dimensional NMR, solid state NMR, and isotopic substitution are also introduced. Characteristics of phosphorylated amino acids and peptides, as revealed by phosphorus-31 NMR, are described. Studies of phosphorylated containing phosphomonoesters, phosphoramidates, acyl phosphates, and disubstituted phosphorus bridges are discussed. Among these phosphoproteins are several examples where phosphorus residues evidently play a role as polyelectrolytes, in enzyme catalysis, and in regulation of protein function.