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Folding and dimerization kinetics of bone morphogenetic protein‐2, a member of the transforming growth factor‐β family
Author(s) -
Vallejo Luis F.,
Rinas Ursula
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12051
Subject(s) - chemistry , kinetics , ionic strength , protein folding , redox , folding (dsp implementation) , bone morphogenetic protein , biophysics , cystine , monomer , crystallography , biochemistry , cysteine , inorganic chemistry , biology , organic chemistry , aqueous solution , physics , quantum mechanics , electrical engineering , gene , engineering , enzyme , polymer
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. Structured digital abstractBMP‐2 and BMP‐2 bind by cross-linking study ( View interaction )