Ft-ir studies of lipid/protein interaction in biological membranes

Richard Mendelsohn, Mark Jaworsky, Gloria Anderle

Research output: Contribution to journalArticlepeer-review


FT-IR spectroscopy has been used to monitor phospholipid order and melting characteristics as well as protein secondary structure in reconstituted membrane systems. The protein used in the current work is CaATPase, a Calcium-pumping protein isolated from rabbit skeletal muscle. The protein is isolated, purified and reconstituted into phospholipid vesicles of the desired composition. High precision (0,03 cm-1) measurements of the temperature dependence of the acyl chain CH2 stretching frequencies are used to construct melting curves for the various phospholipids used in the current work. The effect of CaATPase on lipid order depends upon the. level of unsaturation of the lipid acyl chains, the strongest perturbations being observed for molecules containing one saturated and one unsaturated chain. Use of acyl chain perdeuterated lipids as one component of a binary lipid mixture permits studies of the thermal response of each component in either binary lipid mixtures or ternary complexes composed of two lipids plus protein. The tendencies of this integral membrane protein to preferentially interact with a particular lipid component is noted in several instances.

Original languageEnglish (US)
Pages (from-to)159-160
Number of pages2
JournalProceedings of SPIE - The International Society for Optical Engineering
StatePublished - Dec 20 1985

All Science Journal Classification (ASJC) codes

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Computer Science Applications
  • Applied Mathematics
  • Electrical and Electronic Engineering


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