Sensitivity Enhancement in Transverse Relaxation Optimized NMR Spectroscopy

Angew Chem Int Ed Engl. 1998 Nov 2;37(20):2859-2861. doi: 10.1002/(SICI)1521-3773(19981102)37:20<2859::AID-ANIE2859>3.0.CO;2-4.

Abstract

Dramatically shortened transverse relaxation times in transverse relaxation optimized spectroscopy (TROSY) result from interference between dipole-dipole interactions and the anisotropy of the chemical shift. Thus NMR spectroscopy becomes a suitable method for studying large biomolecules, with optimal performance when 1-GHz spectrometers become available. By using new phase cycles and data-processing methods, the sensitivity of the TROSY experiment was increased by a factor of √2, which is of considerable importance for applications in high-field NMR studies on large proteins.

Keywords: NMR spectroscopy; Proteins.