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Nuclear Magnetic Resonance Spectroscopic Studies of Erythrocyte Membranes

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Abstract

THE nature of molecular interactions in the lipoprotein complexes of biological membranes has been a subject under active enquiry for many years. The classical Davson-Danielli paucimolecular model1 postulates apolar mutual interaction between the lipid molecules and electrostatic binding of the lipid with the structural protein. Although this model has received support from biophysical studies, especially on myelin2,3, there is other experimental evidence which suggests that extensive hydrophobic binding may occur between lipids and proteins, for example, from studies on mitochondria4,5, halobacterium halobium6, erythrocyte ghosts7, plasma membrane fragments of Ehrlich ascites cells (D. F. H. Wallach and P. H. Zahler, personal communication) and chloroplast lamellae8.

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Authors and Affiliations

  1. Molecular Biophysics Unit, Unilever Research Laboratory, The Frythe, Welwyn, Hertfordshire

    D. CHAPMAN, V. B. KAMAT, J. DE GIER & S. A. PENKETT

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  1. D. CHAPMAN
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  2. V. B. KAMAT
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  3. J. DE GIER
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  4. S. A. PENKETT
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CHAPMAN, D., KAMAT, V., DE GIER, J. et al. Nuclear Magnetic Resonance Spectroscopic Studies of Erythrocyte Membranes. Nature 213, 74–75 (1967). https://doi.org/10.1038/213074a0

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