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Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding
Author(s): Timothy L. Tapley, Jan L. Korner, Madhuri T. Barge, Julia Hupfeld, Joseph A. Schauerte, Ari Gafni, Ursula Jakob, James C.A. Bardwell
Professor Matthew Chapman and his lab group offer novel insights into how bacteriaform fibers called curli, giving intriguing clues to the formation of harmful protein tangles in devastating diseases involving aberrant protein folding. In the current work, the researchers reveal details of how curli - functional amyloid fibers assembled by E. coli and certain other bacteria - are assembled. Their results will be published online in the Proceedings of the National Academy of Sciences during the week of July 9-13.
Name of Periodical: PNAS
Year of Publication: 2009