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 Homology-modelled structure of the βB2B3-crystallin heterodimer studied by ion mobility and radical probe MS. Homology-modelled structure of the βB2B3-crystallin heterodimer studied by ion mobility and radical probe MS. FEBS J. (1742-464X) 2011 imex curation Downard KM., Kokabu Y., Ikeguchi M., Akashi S. k.downard@sydney.edu.au Only protein-protein interactions in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Downard KM., Kokabu Y., Ikeguchi M., Akashi S. k.downard@sydney.edu.au FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation crbb3_bovin Beta-crystallin B3 CRYBB3 Beta-B3 crystallin protein protein bovin Bos taurus (Bovine) Bovine MAEQHSTPEQAAAGKSHGGLGGSYKVIVYEMENFQGKRCELTAECPNLTESLLEKVGSIQVESGPWLAFERRAFRGEQYVLEKGDYPRWDAWSNSHHSDSLLSLRPLHIDGPDHKLHLFENPAFGGRKMEIVDDDVPSLWAHGFQDRVASVRAINGTWVGYEFPGYRGRQYVFERGEYRHWNEWDANQPQLQSVRRIRDQKWHKRGVFLSS mint Crystallins are the dominant structural components of the vertebrate eye lens 8D388B3F1785286A crbb2_bovin Beta-crystallin B2 CRYBB2 Beta-B2 crystallin Beta-crystallin Bp protein protein bovin Bos taurus (Bovine) Bovine MASDHQTQAGKPQPLNPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKITLYENPNFTGKKMEVIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSGDFGAPQPQVQSVRRIRDMQWHQRGAFHPSS mint Crystallins are the dominant structural components of the vertebrate eye lens 9613C228491E3C8C crybb2-crybb3 1 Beta-crystallin B2 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Beta-crystallin B3 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction homomint mint f2 f3 f4 Ion mobility of the βB2B3-crystallin heterodimer The ESI-TOF mass spectrum of βL-crystallin recorded under non-denaturing conditions in a solution containing 50mM ammonium acetate buffer (pH 6.8) is shown in Figure 2. The spectrum contains the 13+ and 14+ protonated [M+zH]z+ ions of the βB2B2 homodimer and the βB2B3 heterodimer whose molecular masses are measured to be 46416.6 and 47448.3 respectively. In addition the 8+ and 9+ protonated ions of the βB2 monomer are evident with the mass of this protein measured to be 23208.2. All measured masses are within 20ppm of their theoretical values. Since the βB2 subunit is detected within the homodimer and heterodimer, it is not possible to estimate the dissociation constant (Kd) of the heterodimer from a ratio of the intensities of its ions and those of the βB2 monomer within the mass spectrum [36]. However, since ions for the βB3 monomer were not detected in the spectrum of beta-crystallin at 25uM, the dissociation constant (Kd) of the heterodimer can be estimated to be below this value. The mass spectrum obtained simultaneously with the drift time measurement is very similar to that in Figure 2 albeit with lower mass resolution due to the longer period of time that ions spend in the drift tube at higher pressures. The ion mobilities for each of the major ions were extracted from this data and are also shown in Figure 3. crybb2-1 1 Beta-crystallin B2 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint f2 f3 f4 Ion mobility of the βB2B3-crystallin heterodimer The ESI-TOF mass spectrum of βL-crystallin recorded under non-denaturing conditions in a solution containing 50mM ammonium acetate buffer (pH 6.8) is shown in Figure 2. The spectrum contains the 13+ and 14+ protonated [M+zH]z+ ions of the βB2B2 homodimer and the βB2B3 heterodimer whose molecular masses are measured to be 46416.6 and 47448.3 respectively. In addition the 8+ and 9+ protonated ions of the βB2 monomer are evident with the mass of this protein measured to be 23208.2. All measured masses are within 20ppm of their theoretical values. Since the βB2 subunit is detected within the homodimer and heterodimer, it is not possible to estimate the dissociation constant (Kd) of the heterodimer from a ratio of the intensities of its ions and those of the βB2 monomer within the mass spectrum [36]. However, since ions for the βB3 monomer were not detected in the spectrum of beta-crystallin at 25uM, the dissociation constant (Kd) of the heterodimer can be estimated to be below this value. The mass spectrum obtained simultaneously with the drift time measurement is very similar to that in Figure 2 albeit with lower mass resolution due to the longer period of time that ions spend in the drift tube at higher pressures. The ion mobilities for each of the major ions were extracted from this data and are also shown in Figure 3.