Transverse relaxation-optimized determination

Fushman, D. and D. Cowburn, Nuclear magnetic resonance relaxation in determination of residue-specific 1SN chemical shift tensors in proteins in solution protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy, in Methods Enzymol. T. James, U. Schmitz, and V. Doetsch, Editors. 2001. p.109-126. 

Structure determination. The introduction of transverse relaxation optimized spectroscopy (TROSY) by Wuthrich and co-workers [276] opened up a wealth of new opportunities for solution NMR on large protein systems, including detergent-solubilized membrane proteins. 

A short overlook on transverse relaxation-optimized spectroscopy (TROSY) in combination with various isotope-labelling techniques has been published by Fernandez and Wider. The method improves, among others, the detection of scalar couplings across hydrogen bonds, providing crucial information on the determination of solution structures of large proteins and oligonucleotides. 

During the past two years, significant advances have been made in the development of NMR methods for studying biomolecular dynamics on the microsecond to millisecond timescale. Thuduppathy and HilP reviewed applications of NMR spin relaxation methods for measuring biological motions. Fernandez and Wider discussed transverse relaxation-optimized spectroscopy (TROSY) that promises to further enhance the determination of solution structures of large biomolecules. 

Most methods for determining residual dipolar couplings are based on the measurement of the displacement between cross-peak components in J-coupled spectra. However, for large macromolecules and macromolecular complexes, these methods are often unreliable since differential relaxation can significantly broaden one of the multiplet components and thereby make accurate determination of its position difficult. To overcome this problem, a J-evolved transverse relaxation optimized (JE-TROSY) method has been demonstrated for the determination of one-bond couplings that involves J-evolution of the sharpest crosspeak multiplet component selected in a TROSY experiment . Couplings are measured from the displacement of the TROSY component in the additional J-evolution dimension relative to a zero frequency origin. 

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