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Detergents Modulate Dimerization, but not Helicity, of the Glycophorin A Transmembrane Domain

By Lillian E. Fisher, Donald M. Engelman, James N. Sturgis, Professeur De Recherche Blaise and Systemes MacromoleĆ¢culaires


Understanding how features of the lipid environment such as thickness, fluidity, and composition influence the folding and oligomerization of membrane proteins has been limited by a lack of thermodynamic data (Haltia & Friere, 1995; Killian, 1998; Lee, 1998; Mouritsen & Bloom, 1993; Stowell & Rees, 1995; van Klompenburg et al., 1997). The insolubility of membrane-spanning helices in aqueous solutions complicates investigation of their folding and assembly (Popot & de Vitry, 1990; White & Wimley, 1998), even though their hydrophobic nature facilitates their identication in sequenced genomes (Boyd et al., 1998; Wallin & von Heijne, 1998). New approaches, such as the one presented here, are being developed to identify reversible steps in membrane protein folding pathways and to measure how they are thermodynamically coupled to environmental properties (Booth et al., 1997; Huang et al., 1981; Lau & Bowie, 1997; Sturgis & Robert, 1994). Popot & Engelman (1990) hypothesized that th..

Year: 1999
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