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dc.contributor.authorVallejo, Luis F
dc.contributor.authorRinas, Ursula
dc.date.accessioned2013-04-22T14:40:11Z
dc.date.available2013-04-22T14:40:11Z
dc.date.issued2013-01
dc.identifier.citationFolding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family. 2013, 280 (1):83-92 FEBS J.en_GB
dc.identifier.issn1742-4658
dc.identifier.pmid23122408
dc.identifier.doi10.1111/febs.12051
dc.identifier.urihttp://hdl.handle.net/10033/283572
dc.description.abstractThe 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.
dc.language.isoenen
dc.rightsArchived with thanks to The FEBS journalen_GB
dc.subject.meshBone Morphogenetic Protein 2en_GB
dc.subject.meshBuffersen_GB
dc.subject.meshGlutathione Disulfideen_GB
dc.subject.meshGuanidineen_GB
dc.subject.meshHumansen_GB
dc.subject.meshKineticsen_GB
dc.subject.meshModels, Biologicalen_GB
dc.subject.meshOxidation-Reductionen_GB
dc.subject.meshProtein Denaturationen_GB
dc.subject.meshProtein Foldingen_GB
dc.subject.meshProtein Multimerizationen_GB
dc.subject.meshProtein Stabilityen_GB
dc.subject.meshSodium Chlorideen_GB
dc.subject.meshTGF-beta Superfamily Proteinsen_GB
dc.titleFolding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Braunschweig, Germany.en_GB
dc.identifier.journalThe FEBS journalen_GB
refterms.dateFOA2014-01-15T00:00:00Z
html.description.abstractThe 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.


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