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 The sea anemone actinoporins (Arg-Gly-Asp) conserved motif is involved in maintaining the competent oligomerization state of these pore-forming toxins. The sea anemone actinoporins (Arg-Gly-Asp) conserved motif is involved in maintaining the competent oligomerization state of these pore-forming toxins. FEBS J. (1742-464X) 2014 imex curation García-Linares S., Richmond R., García-Mayoral M.F., Bustamante N., Bruix M., Gavilanes J.G., Martínez-Del-Pozo A. ppgf@bbm1.ucm.es 18-Feb-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined ppgf@bbm1.ucm.es Accepted 2014-JAN-14 by LUANA 2014 imex curation actp2_stihl DELTA-stichotoxin-She4b Cytolysin III Sticholysin II Sticholysin-2 protein protein stohe Stoichactis helianthus ALAGTIIAGASLTFQVLDKVLEELGKVSRKIAVGIDNESGGTWTALNAYFRSGTTDVILPEFVPNTKALLYSGRKDTGPVATGAVAAFAYYMSSGNTLGVMFSVPFDYNWYSNWWDVKIYSGKRRADQGMYEDLYYGNPYRGDNGWHEKNLGYGLRMKGIMTSAGEAKMQIKISR B50566B02D351B1D actp2 1 StnII 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified RAD mutant (G142A) direct interaction direct interaction f3 Sedimentation velocity (560 μM protein concentration in water) experiments were conducted (Fig. 3). The sedimentation coefficients obtained for the StnII RAD mutant in these conditions indicated the presence of different species into the sample: monomer (s20,w= 2.2 S, 56%), dimer (s20,w= 3.1 S, 42%,) and tetramer (s20,w= 5.25 S, 2%), suggesting an aggregating prone behaviour of this mutant in solution. Not surprisingly, equilibrium sedimentation analysis of this same sample after an almost 40-fold dilution (15 μM protein concentration) yielded results compatible with only a single monomer species (Fig. 3) with an average molecular mass (MWapp) of 20.7 ± 0.7 kDa (average of all velocities assayed). actp2-1 1 StnII 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified RAD mutant (G142A) direct interaction direct interaction f3 Sedimentation velocity (560 μM protein concentration in water) experiments were conducted (Fig. 3). The sedimentation coefficients obtained for the StnII RAD mutant in these conditions indicated the presence of different species into the sample: monomer (s20,w= 2.2 S, 56%), dimer (s20,w= 3.1 S, 42%,) and tetramer (s20,w= 5.25 S, 2%), suggesting an aggregating prone behaviour of this mutant in solution. Not surprisingly, equilibrium sedimentation analysis of this same sample after an almost 40-fold dilution (15 μM protein concentration) yielded results compatible with only a single monomer species (Fig. 3) with an average molecular mass (MWapp) of 20.7 ± 0.7 kDa (average of all velocities assayed).