In the assembly pathway of the trimeric P22 tailspike protein, the protein conformation critical for the parti-tioning between productive folding and off-pathway ag-gregation is a monomeric folding intermediate. The cen-tral domain of tailspike, a large right-handed parallel b-helix, is essentially structured in this species. We used the isolated b-helix domain (Bhx), expressed with a hexahistidine tag, to investigate the mechanism of ag-gregation without the two terminal domains present in the complete protein. Although Bhx has been shown to fold reversibly at low ionic strength conditions, in-creased ionic strength induced aggregation with a max-imum at urea concentrations corresponding to the mid-point of urea-induced folding transitions. According to size exclusion chromatography, aggregation appeare
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