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• W2078561353 abstract "Erythrocyte membranes prepared from human red blood cells by hypotonic lysis, contain protein in a mixture of α helical and “unordered” conformations. Using infrared absorption spectroscopy we have demonstrated that in the presence of adenosine triphosphate and Mg2+, the protein in these membranes undergoes a transition to an anti-parallel β structure, which is enhanced by the addition of Na+ and K+. This transition can be prevented or reversed under conditions which inhibit the adenosine triphosphatase reaction. The results are discussed in the light of data previously obtained by infrared spectroscopy on rat liver mitochondria, in terms of a generalized membrane-energy transduction concept." @default.
• W2078561353 created "2016-06-24" @default.
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• W2078561353 date "1971-07-01" @default.
• W2078561353 modified "2023-10-18" @default.
• W2078561353 title "Protein conformational transitions in the erythrocyte membrane" @default.
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• W2078561353 doi "https://doi.org/10.1016/0005-2736(71)90315-4" @default.
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