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

Joseph A. Goncalves, Shivani Ahuja, Sina Erfani, Markus Eilers, Steven O. Smith

Research output: Contribution to journalReview articlepeer-review

36 Scopus citations


The progress that has been made using NMR spectroscopy to characterize the structure and dynamics of G-protein-coupled receptors (GPCRs) in membrane environments are discussed. The seven-transmembrane helix GPCRs have evolved to recognize and transduce signals as diverse as light, Ca2+, small organic molecules and proteins. There are several areas where NMR can have an impact on understanding the structure and function of GPCRs. These include ligand conformation and interactions, molecular mechanisms of activation switches, role of water in activation; and role of the membrane in activation. Dynamic nuclear polarization (DNP) is an application, using microwave irradiation to polarize spin labels and transfer the resulting magnetization to NMR spins of interest. When applied to a 13C-labeled rhodopsin sample, DNP results in a <20-fold increase in sensitivity. As a result, the method opens up the possibility of structural studies on >1 mg of expressed and functional GPCRs.

Original languageEnglish
Pages (from-to)159-180
Number of pages22
JournalProgress in Nuclear Magnetic Resonance Spectroscopy
Issue number2
StatePublished - Aug 2010


  • Magic angle spinning
  • Membrane proteins
  • Structure


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