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. Using these procedures, the energetics and pathways of folding, as well as the existence of transient intermediate states between unfolded and fully folded polypeptides, have been characterized for a number of proteins (for a collection of reviews, see Creighton, 1992; Pain, 1994)
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. Therefore, the respective unfolded states can have rather different structures (21)
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. As we discussed previously (13), the behavior in this study is relevant to globular proteins subjected to osmotic stress in biological situations
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. On the other hand, seeding experiments suggest that mature, solid fibrils act as the most effective catalysts of amyloidogenesis in vitro (Harper et al
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. Due to the complexity of the investigated proteins (multitryptophan proteins in an ensemble of structurally heterogeneous unfolded states) a quantitative relation between λ^sub max^-values and the extent of aggregation or the compactness of the unfolded state cannot be given
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