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    Folding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family.

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    Authors
    Vallejo, Luis F
    Rinas, Ursula
    Issue Date
    2013-01
    
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    Abstract
    The kinetics of folding and dimerization of bone morphogenetic protein-2 (BMP-2), a disulfide-connected, homodimeric cystine-knot protein and a member of the transforming growth factor-β superfamily, was analyzed under a variety of different conditions. Refolding and dimerization of BMP-2 were extremely slow under all conditions studied, and could be described by consecutive first-order reactions involving at least one long-lived intermediate. The rate constants vary from ~ 0.2 × 10(-5) to ~ 3.5 × 10(-5) s(-1), and were strongly dependent on temperature, redox conditions, and the presence of stabilizing or destabilizing ions. In particular, the combined impact of ionic strength and redox conditions on the rates indicates that electrostatic interactions control thiol-disulfide exchange reactions on the path from the unfolded and reduced monomers to the disulfide-connected growth factor in a rate-determining way.
    Citation
    Folding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family. 2013, 280 (1):83-92 FEBS J.
    Affiliation
    Helmholtz Centre for Infection Research, Braunschweig, Germany.
    Journal
    The FEBS journal
    URI
    http://hdl.handle.net/10033/283572
    DOI
    10.1111/febs.12051
    PubMed ID
    23122408
    Type
    Article
    Language
    en
    ISSN
    1742-4658
    ae974a485f413a2113503eed53cd6c53
    10.1111/febs.12051
    Scopus Count
    Collections
    publications of the research group recombinant protein expression (RPEX)

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