Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy

Olivier Soubias; Klaus Gawrisch

doi:10.1021/ja0538942

Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy

J Am Chem Soc. 2005 Sep 28;127(38):13110-1. doi: 10.1021/ja0538942.

Authors

Olivier Soubias¹, Klaus Gawrisch

Affiliation

¹ Laboratory of Membrane Biochemistry and Biophysics, NIAAA, National Institutes of Health, Bethesda, Maryland 20892, USA.

PMID: 16173715
DOI: 10.1021/ja0538942

Abstract

We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the polyunsaturated docosahexaenoic acid.

Publication types

Research Support, N.I.H., Intramural

MeSH terms

Animals
Cattle
Glycerylphosphorylcholine / analogs & derivatives*
Glycerylphosphorylcholine / chemistry
Nuclear Magnetic Resonance, Biomolecular / methods*
Rhodopsin / chemistry*

Substances

1-palm-itoyl-d31-2-oleoyl-sn-glycero-3-phosphocholine
1-stearoyl-d35-2-docosahexaenoyl-sn-glycero-3-phosphocholine
Glycerylphosphorylcholine
Rhodopsin

Grants and funding

Intramural NIH HHS/United States