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Folding and amyloid-fibril formation for a series of human stefins' chimeras: any correlation?
Kenig, Manca ...
To study the influence of whole secondary structure elements to the process offolding and amyloid-fibril formation, chimeras of stefins have been prepared. GdnHCl denaturation curves and folding ...rates (chevron plots) have been analyzed based on a two-state mechanism. The order of stability isČ stefin A > aAbbbb > bAbbbb > stefin B = aBaaaa > bBaaaa, where the make up of chimeric proteins is designated by small letters representing the source of individual strands (a for stefin A, b for stefin B) and a capital letter representing the source of the helix (A for stefin A and B for stefin B). Onlythe fast folding reactions were included in the analysis and it has been found that stefin B folds the fastest (657 s-1). Similarly, fast folders are the chimeric proteins aBaaaa and bBaaaa, both of which contain the -helix of stefin B. Unfolding rates correlate very well with protein stability, with theslowest rate for the most stable protein, stefin A. Amyloid-fibril growth was measured for each protein by monitoring thioflavin T fluorescence and was visualized using electron microscopy. The propensity to form amyloid-fibrils is in the orderČ stefin B > bAbbbb > aAbbbb > bBaaaa > aBaaaa > stefin A. Thisorder does not correlate with stability, or with the folding or unfolding rates. Instead, the propensity to fibrillize is related to selected parts of structure, such as the -sheet of stefin B, and can be predicted reasonably well by calculating the -strand propensity of the denatured states.
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