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

2.50
Hdl Handle:
http://hdl.handle.net/10033/283572
Title:
Folding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family.
Authors:
Vallejo, Luis F; Rinas, Ursula
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.
Affiliation:
Helmholtz Centre for Infection Research, Braunschweig, Germany.
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.
Journal:
The FEBS journal
Issue Date:
Jan-2013
URI:
http://hdl.handle.net/10033/283572
DOI:
10.1111/febs.12051
PubMed ID:
23122408
Type:
Article
Language:
en
ISSN:
1742-4658
Appears in Collections:
publications of the research group recombinant protein expression (RPEX)

Full metadata record

DC FieldValue Language
dc.contributor.authorVallejo, Luis Fen_GB
dc.contributor.authorRinas, Ursulaen_GB
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.en_GB
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
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