Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold.

Y.J.M. Bollen, C.P.M. van Mierlo

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    The topology of a native protein influences the rate with which it is formed, but does topology affect the appearance of folding intermediates and their specific role in kinetic folding as well? This question is addressed by comparing the folding data recently obtained on apoflavodoxin from Azotobacter vinelandii with those available on all three other α-β parallel proteins the kinetic folding mechanism of which has been studied, i.e. Anabaena apoflavodoxin, Fusarium solani pisi cutinase and CheY. Two kinetic folding intermediates, one on-pathway and the other off-pathway, seem to be present during the folding of proteins with an α-β parallel, also called flavodoxin-like, topology. The on-pathway intermediate lies on a direct route from the unfolded to the native state of the protein involved. The off-pathway intermediate needs to unfold to allow the production of native protein. Available simulation data of the folding of CheY show the involvement of two intermediates with characteristics that resemble those of the two intermediates experimentally observed. Apparently, protein topology governs the appearance and kinetic roles of protein folding intermediates during the folding of proteins that have a flavodoxin-like fold. © 2004 Elsevier B.V. All rights reserved.
    Original languageEnglish
    Pages (from-to)181-189
    JournalBiophysical Chemistry
    Volume114
    DOIs
    Publication statusPublished - 2005

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