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Updated: Aug 23, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding
Guang Zhu1, Youlin Xia, Donghai Lin
1Department of Biochemistry, The Hong Kong University of Science and Technology, Hong Kong, SAR People's Republic of China.
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.
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