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• W285009388 abstract "This chapter describes the structure–function relations in band 3 protein. The arrangement of band 3 polypeptides involved in red blood cell anion transport has been studied with a variety of labeling and cleaving agents. The single anion transport site present in each polypeptide is formed by interactions between two transmembrane fragments of the polypeptide. The interactions could be apparently modified membrane fluidity. The site is located in a niche which, although close to the external surface, is buried within the protein. It comprises a variety of positively charged amino acids, possibly also a negatively charged group and an electron donor group within a hydrophobic pocket. The sites are accessible from either surface by anionic water-soluble agents, leaving the hypothetical barrier as a rather small domain, comprising only a fraction of the membrane's anatomical width. Transport is envisioned as a small conformational change over the above barrier." @default.
• W285009388 created "2016-06-24" @default.
• W285009388 creator A5064972013 @default.
• W285009388 date "1983-01-01" @default.
• W285009388 modified "2023-09-23" @default.
• W285009388 title "STRUCTURE-FUNCTION RELATIONS IN BAND 3 PROTEIN" @default.
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• W285009388 doi "https://doi.org/10.1016/b978-0-444-80540-9.50036-4" @default.
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