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The highly dynamic conformational state formed by the protein domain HypF-N at low pH, before aggregation, is examined by using fluorescence, circular dichroism and NMR spectroscopies. The studies have shown that strategies solely based on the characterization of the partially unfolded states populated before aggregation are unlikely to provide a detailed description of the mechanism of aggregation.

The sequence and structural determinants of protein aggregation in amyloid fibril formation and the factors that dominate the aggregation of unfolded peptides and proteins is described. The factors that pertain to the aggregation of partially structured states are reviewed and the ability of the even fully folded proteins states to aggregate into early oligomers in any case with no need to undergo significant conformational changes are presented.