13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67 degrees C for 5 minutes [YashRoy, R.C. (1991) J. Biochem. Biophys. Methods 22, 55-59]. Line-broadening of 13C-NMR resonances arising from the 1st (carbonyl), 7th, 9th and 12th carbon atom of fatty-acyl chains with reference to the carbonyl (C-1) group shows increased immobilization of lipid fatty-acyl chains at these locations, obviously caused by changes in interactions between membrane lipids and proteins upon heat denaturation of membrane proteins.
YashRoy
R C
RC
Biology Department, Carleton University, Ottawa, Canada.
D002247:Carbon Isotopes; D002736:Chloroplasts / Q000378:metabolism; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D011489:Protein Denaturation / Q000502:physiology; D014675:Vegetables / Q000378:metabolism
D002247:Carbon Isotopes; D008563:Membrane Lipids; D008565:Membrane Proteins