NMR of Protein-Lipid Interactions in Model and Biological Membrane Systems

  • Eric Oldfield


Membranes are composed predominantly of lipids, proteins, and sterol molecules and are responsible at least in part for a wide variety of biochemical processes such as respiration, vision, photosynthesis, cell-cell recognition, and nerve impulse transmission. Not surprisingly then, there have been considerable efforts spent in attempting to characterize the molecular structure of, and intermolecular interactions between, individual membrane components, in an attempt to relate the structures of membranes to their function. In this short review we discuss recent developments in our understanding of the structure of membranes obtained by means of NMR spectroscopic techniques. We show that protein-lipid interactions in both model and intact biological membranes are characterized by a dynamic disordering of boundary-lipid hydrocarbon chains, as viewed by high-field deuterium NMR spectroscopy, while 31P spectra indicate significant disordering and/or immobilization within the phospholipid polar head group region due to association with protein. The effects are very different from those seen with cholesterol, and are in marked contrast to the old ideas of rigid, ordered “boundary-lipid” surrounding membrane proteins. We also present results suggesting that it will soon be possible to directly monitor the effects of lipid on protein dynamics by means of NMR spectroscopy.


Phase Transition Temperature Quadrupole Splitting Purple Membrane Pure Lipid Halobacterium Halobium 
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Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Eric Oldfield
    • 1
  1. 1.School of Chemical SciencesUniversity of IllinoisUrbanaUSA

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