The general relations between protein conformation and the optical activity of peptide chromophores are outlined and applied to the analysis of the optical rotatory dispersion and circular dichroism of the plasma membranes of human erythrocytes and Ehrlich ascites carcinoma cells. It is concluded that the proteins of these membranes are "globular" and that they have considerable helical content. The spectroscopic consequences of perturbing the membranes with phospholipase C, phospholipase A, lysolecithin, and sodium dodecyl sulfate are examined in the light of the effects of these agents upon certain enzymatic and physical properties of the membranes and upon their proton magnetic resonance spectra. The data suggest that the architecture of membrane proteins is strongly dependent upon apolar lipid-protein and/or lipid-sensitive protein-protein interactions.
Article| July 01 1969
Membrane Lipids and the Conformations of Membrane Proteins
Donald F. H. Wallach
From the Biochemical Research Laboratory, Massachusetts General Hospital, and the Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02114
Online Issn: 1540-7748
Print Issn: 0022-1295
Copyright © 1969 by The Rockefeller University Press
J Gen Physiol (1969) 54 (1): 3–26.
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Donald F. H. Wallach; Membrane Lipids and the Conformations of Membrane Proteins . J Gen Physiol 1 July 1969; 54 (1): 3–26. doi: https://doi.org/10.1085/jgp.54.1.3
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