Combined solid state and solution NMR studies of α,ε-15N labeled bovine rhodopsin

Karla Werner, Ines Lehner, Harpreet Kaur Dhiman, Christian Richter, Clemens Glaubitz, Harald Schwalbe, Judith Klein-Seetharaman, Gobind H. Khorana

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Rhodopsin is the visual pigment of the vertebrate rod photoreceptor cell and is the only member of the G protein coupled receptor family for which a crystal structure is available. Towards the study of dynamics in rhodopsin, we report NMR-spectroscopic investigations of α,ε-15N-tryptophan labeled rhodopsin in detergent micelles and reconstituted in phospholipids. Using a combination of solid state 13C,15N-REDOR and HETCOR experiments of all possible 13C′i-1 carbonyl/ 15Ni-tryptophan isotope labeled amide pairs, and H/D exchange 1H,15N-HSQC experiments conducted in solution, we assigned chemical shifts to all five rhodopsin tryptophan backbone 15N nuclei and partially to their bound protons. 1H,15N chemical shift assignment was achieved for indole side chains of Trp351.30 and Trp1754.65. 15N chemical shifts were found to be similar when comparing those obtained in the native like reconstituted lipid environment and those obtained in detergent micelles for all tryptophans except Trp1754.65 at the membrane interface. The results suggest that the integrated solution and solid state NMR approach presented provides highly complementary information in the study of structure and dynamics of large membrane proteins like rhodopsin.

Original languageEnglish (US)
Pages (from-to)303-312
Number of pages10
JournalJournal of Biomolecular NMR
Issue number4
StatePublished - Apr 2007
Externally publishedYes


  • GPCR
  • HSQC
  • Membrane proteins
  • Rhodopsin
  • Tryptophan

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy


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