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Fig. 5. (A) Dependence of the solubility of deoxy HbS upon dextran concentration (Bookchin et al., 1999). A 1.75-fold increase in dextran concentration results in a greater than four-fold increase in the equilibrium tendency of deoxy HbS to polymerize. (B) Time course of assembly of HIV capsid protein in the absence (
) and presence (
) of 100 g/l Ficoll 70 (del Alamo, 2005). The half-time for assembly of the protein is decreased ten-fold in the presence of Ficoll. (C) Temperature dependence of the ellipticity of 
-lactalbumin in bulk solution (
) and encapsulated in hydrated silica sol-gel glass (
). The confined protein behaves normally at low temperature, but exhibits only partial unfolding even at temperatures approaching 100°C. Figure reproduced with permission from Eggers and Valentine (Eggers and Valentine, 2001). (D) Time dependence of adsorption of several unrelated proteins to a supported phospholipid bilayer (symbols and solid curves) (Fernandez and Berry, 2003). The dotted curves indicate the time dependence that would be expected in the absence of interaction between adsorbed proteins. The enhanced steepness of the experimentally observed curves (solid) relative to the reference curves (dotted) indicates self-association resulting in clustering of the adsorbed proteins (Minton, 2001b).
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