Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 342697
Title Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold
Author(s) Bollen, Y.J.M.; Mierlo, C.P.M. van
Source Biophysical Chemistry 114 (2005)2-3. - ISSN 0301-4622 - p. 181 - 189.
Department(s) Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) azotobacter-vinelandii apoflavodoxin - transition-state - pathway - mechanisms - kinetics - steps - chey
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 ¿-ß 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 ¿-ß 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.
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