2-DIMENSIONAL SPIN-ECHO CORRELATED SPECTROSCOPY (SECSY) FOR H-1-NMR STUDIES OF BIOLOGICAL MACROMOLECULES

The principle and the experimental realization of spin echo correlated spectroscopy (SECSY) are described and its use for studies of proteins is illustrated with 1H n.m.r. spectra of the basic pancreatic trypsin inhibitor. This technique yields two-dimensional homonuclear correlated spectra which manifest connectivities between spin coupled nuclei and thus provide first level assignments of individual spin systems in biopolymers. Compared to previously described two-dimensional correlated n.m.r. techniques, which were applied exclusively to small molecules, SECSY uses a smaller data size both in the time domain and the frequency domain, which makes it particularly suitable for studies of macromolecules. © 1979.