Raman and Fourier transform infrared spectroscopic studies of the interaction between glycophorin and dimyristoylphosphatidylcholine

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1021/bi00526a027
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Name affiliation
  1. National Research Council Canada
FormatText
TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume20
Issue23
Pages6699–6706
Abstract
Glycophorin from the human erythrocyte membrane has been isolated in pure form and reconstituted into large unilamellar vesicles with 1,2-dimyristoy1-3-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 phase 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 (~5ºC) or in the liyuid-crystalline phase.
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LanguageEnglish
Peer reviewedYes
NRC number19425
NPARC number23001733
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Record identifier44ebddd3-62b7-4f75-ae34-2f1d2b5f9b16
Record created2017-03-24
Record modified2017-03-24
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