TROSY NMR for Studies of Large Biological Macromolecules in Solution

Abstract

Transverse relaxation-optimized spectroscopy (TROSY), in combination with isotope labeling techniques and with improvements in NMR instrumentation, have greatly extended applications of NMR spectroscopy to large biological macromolecules that were otherwise not accessible to high-resolution solution state NMR. Important recent applications of TROSY include the structure determinations of integral membrane proteins in detergent micelles, structural and functional studies of large proteins in monomeric form and in macromolecular complexes, and investigations of intermolecular interactions in large complexes. Moreover, TROSY can improve measurements of NMR parameters, such as residual dipolar couplings and scalar couplings across hydrogen bonds, which contribute to a further improvement of the quality and the precision of solution structures of large proteins and oligonucleotides.