Structure and function of G protein-coupled receptors using NMR spectroscopy

NMR Spectroscopy for Studying Interactions of Bioactive Molecules

“…Goncalves et al [117] reviewed a recent development in NMR methods for the structural characterisation of G protein-coupled receptors. This review outlines three key NMR interactions that yield structural information on G proteincoupled receptors: a) chemical shifts that provide information on the local environment, conformational changes and hydrogen bonding, b) dipolar couplings used to measure internuclear distances and orientations, c) quadrupolar couplings that are sensitive to molecular motion.…”

Chapter 2. Insights into GPCR Activation from NMR Spectroscopy

“…140 In solid-state MAS NMR measurements of 13 C-labeled rhodopsin, DNP has provided 420-fold increases in sensitivity. 141 As a result, the method opens up the possibility of structural studies on o1 mg of expressed and functional GPCRs. Furthermore, with the success of using engineered and constitutively active mutants for crystallization, there promises to be a number of crystal structures available that will provide the starting points for NMR studies in membrane environments.…”

NMR techniques in biomedical and pharmaceutical analysis

“…Even human, porcine and bovine insulin, consisting of 51 amino acids and differing in only 4, can be distinguished by their NMR spectra [140]. Furthermore, NMR spectroscopy has become a routine technology for protein characterization, not only for small proteins such as enzymes but also for large proteins like G protein-coupled receptors (for review see [141]). …”