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. The amide I' hand of native ACYI in the original IR spectrum (Fig
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. This two-stage scheme is similar to that from the chemical unfolding/ refolding studies of ACYI (18,19), which also indicated that there existed a dimeric, aggregation-prone folding intermediate
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. Although gSBA unfolded via a two-state process without the formation of any unfolding intermedialcs, the denaturation profile of rSBA was poputated with an intermediate (Fig
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. Interpretations suggesting that highly denatured proteins might he embryos of their native-state counterparts must he treated with extreme caution because there is no sound theoretical basis for such proposals
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. Is there or isn't there? The case for (and against) residual structure in chemically denatured proteins
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. Compared to affinities of 0
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. The presence of exchange between multiple-target sites and flexibility in the bound state leads to an important advantage over rigid binding, namely that the affinity (and specificity) is finely tuned
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. At lower pHs an increase in ionic strength screens the electrostatic repulsion of positive charges on the monomer and stabilizes the dimer (25,26)
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. Although different distribution profiles of fibrillar features may still be explained in terms of kinetic effects (temperature may differently affect the kinetics at various stages of the assembly, effectively marginalizing certain sequential processes), the higher temperature may also have a more direct effect on amyloidogenesis, for instance by increasing the thermal energy of the interacting molecules and hence causing the alignment of protofilaments to become less accurate
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. Such unspecific effects may contribute to morphological differences in any protein's amyloid samples induced at high temperature
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. Several are located in the putative trimerization interface, S243, C378, and 1439, and two of them, V255 and L260, are located in the β-turn that connects the inner and outer domains of gp120
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. Increasing the molecular weight of the IPP polymer did not significantly change T^sub g^
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. These differences were not statistically significant (p > 0
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. Histology and electron microscopy confirm these findings, indicating that pellets maintained in DMEM/ITS+/TGF-[beta]1 possessed an extensive extracellular matrix (Fig
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