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Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike betahelix domain

By Benjamin Schuler, Reinhard Rachel and Robert Seckleri


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

Year: 1999
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