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 386373
Title Topological switching between an a-ß parallel protein and a remarkably helical molten globule.
Author(s) Nabuurs, S.M.; Westphal, A.H.; Toorn, M. aan den; Lindhoud, S.; Mierlo, C.P.M. van
Source Journal of the American Chemical Society 131 (2009)23. - ISSN 0002-7863 - p. 8290 - 8295.
DOI https://doi.org/10.1021/ja9014309
Department(s) Biochemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2009
Keyword(s) azotobacter-vinelandii apoflavodoxin - pathway folding intermediate - structural-characterization - on-pathway - unfolded molecules - hydrogen-exchange - energy landscape - flavodoxin-ii - state - apomyoglobin
Abstract Partially folded protein species transiently exist during folding of most proteins. Often these species are molten globules, which may be on- or off-pathway to native protein. Molten globules have a substantial amount of secondary structure but lack virtually all the tertiary side-chain packing characteristic of natively folded proteins. These ensembles of interconverting conformers are prone to aggregation and potentially play a role in numerous devastating pathologies, and thus attract considerable attention. The molten globule that is observed during folding of apoflavodoxin from Azotobacter vinelandii is off-pathway, as it has to unfold before native protein can be formed. Here we report that this species can be trapped under nativelike conditions by substituting amino acid residue F44 by Y44, allowing spectroscopic characterization of its conformation. Whereas native apoflavodoxin contains a parallel ß-sheet surrounded by a-helices (i.e., the flavodoxin-like or a-ß parallel topology), it is shown that the molten globule has a totally different topology: it is helical and contains no ß-sheet. The presence of this remarkably nonnative species shows that single polypeptide sequences can code for distinct folds that swap upon changing conditions. Topological switching between unrelated protein structures is likely a general phenomenon in the protein structure universe
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