Abstract
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) |
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Pages (from-to) | 161-184 |
Number of pages | 24 |
Journal | Methods in molecular biology (Clifton, N.J.) |
Volume | 278 |
State | Published - 2004 |