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Structural mapping of an aggregation nucleation site in a molten globule intermediate


, : Structural mapping of an aggregation nucleation site in a molten globule intermediate. Journal of Biological Chemistry 274(46): 32897-32903

Protein aggregation plays an important role in biotechnology and also causes numerous diseases. Human carbonic anhydrase II is a suitable model protein for studying the mechanism of aggregation. We found that a molten globule state of the enzyme formed aggregates. The intermolecular interactions involved in aggregate formation were localized in a direct way by measuring excimer formation between each of 20 site-specific pyrene-labeled cysteine mutants. The contact area of the aggregated protein was very specific, and all sites included in the intermolecular interactions were located in the large beta-sheet of the protein, within a limited region between the central beta-strands 4 and 7. This substructure is very hydrophobic, which underlines the importance of hydrophobic interactions between specific beta-sheet containing regions in aggregate formation.

US$19.90

PMID: 10551854

DOI: 10.1074/jbc.274.46.32897


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