Rhodopsin exhibits a preference for solvation by polyunsaturated docosohexaenoic acid

Scott E. Feller, Klaus Gawrisch, Thomas B. Woolf

Research output: Contribution to journalArticlepeer-review

86 Scopus citations


An all-atom molecular dynamics simulation of rhodopsin in a membrane environment has been carried out with lipid composition similar to that of the retinal membrane. The initial conformation of the protein was taken from the X-ray crystallographic structure (1F88), while those of the lipids came from a previous molecular dynamics simulation. During the course of the 12.5 ns simulation, the initially randomly placed lipids adopt an anisotropic solvation structure around the protein. The lipids, having one saturated stearic acid chain and one polyunsaturated docosohexaenoic acid chain with a zwitterionic phosphatidylcholine headgroup, arrange themselves to maximize contact between the polyunsaturated chain and the protein surface. This organization is driven by energetically favorable interactions between the transmembrance helices and the docosohexaenoyl chains that are largely of the van der Waals type. These observations are consistent with various experimental studies on rhodopsin and other G-protein coupled receptors and with the picture of extreme flexibility in polyunsaturated fatty acid chains that has arisen from recent NMR and computational work.

Original languageEnglish (US)
Pages (from-to)4434-4435
Number of pages2
JournalJournal of the American Chemical Society
Issue number15
StatePublished - Apr 16 2003

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Rhodopsin exhibits a preference for solvation by polyunsaturated docosohexaenoic acid'. Together they form a unique fingerprint.

Cite this