MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Folding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family. Folding and dimerization kinetics of bone morphogenetic protein-2, a member of the transforming growth factor-β family. FEBS J. (1742-464X) 2013 Vallejo LF., Rinas U. in vitro In vitro crosslink cross-linking study crosslink experimental particp experimental participant identification experimental particp Vallejo LF., Rinas U. FEBS J. (1742-464X) 2013 bmp2_human Bone morphogenetic protein 2 BMP2 BMP2A Bone morphogenetic protein 2A protein protein human Homo sapiens Human MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR DIP protein P12643 original sequence version: 173 DIP protein P12643 original sequence version: 172 DIP protein P12643 original sequence version: 159 DIP protein P12643 original sequence version: 178 20653A3987B25E60 bmp2-1 1 BMP-2 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint Refolding and dimerization of BMP-2 is a very slow process under all conditions studied which can 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 are 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 are controlling thiol-disulfide exchange reactions on the path from the unfolded and reduced monomers to the disulfide-connected growth factor in a ratedetermining way. f1 f3 f4 f5 f6 f7 f8 Supplementary figure 1A : data were used for modeling purposes.