Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.
|Original language||English (US)|
|Number of pages||24|
|Journal||Methods in molecular biology (Clifton, N.J.)|
|State||Published - 2004|