Measurement of one-bond 1Hα-13Cα couplings in backbone-labelled proteins.

NMR dipole-dipole couplings between protein backbone nuclei (¹H^α, ¹³C^α, ¹⁵N, ¹H^N,¹³C′) offer enormous scope for the rapid determination of protein global folds. Here, we show that measurement of one-bond splittings in the protein backbone is facilitated by use of protein that is selectively isotopically enriched only in the backbone atoms. In particular, ¹H^α-¹³C^α couplings can be measured simply and with high sensitivity by use of conventional heteronuclear single quantum correlation (HSQC) techniques. [ABSTRACT FROM AUTHOR]