Solution conformations and dynamics of arginine side chains in a protein deduced from three-bond 15N-1H coupling constants. Cai, Mengli; Huang, Ying; Prakash, Om; Wen, Lisa; Han, Sang Kyou; Krishnamoorthi, Ramaswamy. Department of Biochemistry, Kansas State University, Manhattan, KS, USA. J. Magn. Reson., Ser. B (1995), 108(2), 189-91.

Abstract

The utility of heteronuclear three-bond coupling between 15N and 1H to measure arginine side chain dynamics is demonstrated for those cases where chem. shift degeneracy or cross-peak overlap occurs in homonuclear coupling const. patterns. Uniformly 15N-labeled recombinant Cucurbita maxima trypsin inhibitor-V was used as an example.