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.
Department of Biochemistry, The Hong Kong University of Science and Technology, Hong Kong, SAR People's Republic of China.
Guang
G
Zhu
Youlin
Y
Xia
Donghai
D
Lin
Xiaolian
X
Gao
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