TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding.
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.
Zhu
Guang
G
Department of Biochemistry, The Hong Kong University of Science and Technology, Hong Kong, SAR People's Republic of China.
Xia
Youlin
Y
Lin
Donghai
D
Gao
Xiaolian
X
D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D009696:Nucleic Acids / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*
D046911:Macromolecular Substances; D009696:Nucleic Acids; D011506:Proteins