Protein-lipid interaction

Differential scanning calorimetry, fluorescence spectroscopy and freeze-fracture electron microscopy have been applied to a study of the reconstituted Ca2+-ATPase proteins from sarcoplasmic reticulum when they are incorporated into pure lipid/water systems

Juan C. Gomez-Fernandez

2003

Scholarcy highlights

  • Differential scanning calorimetry, fluorescence spectroscopy and freeze-fracture electron microscopy have been applied to a study of the reconstituted Ca2+-ATPase proteins from sarcoplasmic reticulum when they are incorporated into pure lipid/water systems
  • The results obtained with these techniques have been used to examine the effects of this intrinsic protein upon the surrounding lipid at temperatures above and below the main lipid solid-fluid phase transition temperature
  • This Tc value, the freeze-fracture data show that the proteins are randomly distributed within the plane of the bilayer
  • Tc the proteins occur in high protein to lipid patches, separate from the remaining crystalline lipid
  • The fluorescence data indicate that at these temperatures the presence of the protein causes a decrease in microviscosity, whilst the calorimetric data indicate a decrease in enthalpy of the main lipid transition
  • Transition temperature-ATPase ethyleneglycol bis(β-aminoethyl ether)-N,N′-tetraacetic acid fluorescence polarisation defined as I| − I⊥I| + I⊥, in which I| and I⊥ are the intensities observed parallel and perpendicular, respectively, to an arbitrary axis

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