Raman and Fourier transform infrared spectroscopic studies of the interaction between glycophorin and dimyristoylphosphatidylcholine.
Glycophorin from the human erythrocyte membrane has been isolated in pure form and reconstituted into large unilamellar vesicles with 1,2-dimyristoyl-3-sn-phosphatidylcholine at lipid/protein mole ratios ranging from 50:1 to 200:1. The effect of protein on the phospholipid phase transition has been monitored by Raman and Fourier transform infrared spectroscopy and differential scanning calorimetry. No evidence for an immobilized higher melting lipid component is observed. The gel to liquid-crystalline phas transition is significantly broadened and shifted to lower temperatures as the proportion of protein is increased, while the pretransition is abolished. At all temperatures, the mobility of the acyl chains is increased by the addition of protein while interchain lateral interactions are disrupted. However, there is no evidence for a significant change in the conformational order at low temperatures (approximately 5 degrees C) or ii the liquid-crystalline phase.
D001665:Binding Sites; D002152:Calorimetry, Differential Scanning; D005583:Fourier Analysis; D006021:Glycophorins / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008854:Microscopy, Electron; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011663:Pulmonary Surfactants / Q000378:metabolism*; D012795:Sialoglycoproteins / Q000378:metabolism*; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D013696:Temperature
D006021:Glycophorins; D011663:Pulmonary Surfactants; D012795:Sialoglycoproteins