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 Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. FEBS J. (1742-464X) 2009 Banerjee M., Balaram H., Balaram P. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Banerjee M., Balaram H., Balaram P. FEBS J. (1742-464X) 2009 Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. FEBS J. (1742-464X) 2009 Banerjee M., Balaram H., Balaram P. in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Banerjee M., Balaram H., Balaram P. FEBS J. (1742-464X) 2009 Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. Structural effects of a dimer interface mutation on catalytic activity of triosephosphate isomerase. The role of conserved residues and complementary mutations. FEBS J. (1742-464X) 2009 Banerjee M., Balaram H., Balaram P. in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Banerjee M., Balaram H., Balaram P. FEBS J. (1742-464X) 2009 tpis_plafa Triosephosphate isomerase TPI Triose-phosphate isomerase protein protein plafa Plasmodium falciparum MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM mint EFC8A4373EA9BED1 tpi-1 1 TIM 4 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 F3 mint At a protein concentration of 40 CM, a single band is observed, with an elution volume of 13.9 ml, corresponding to a dimeric enzyme (54 kDa) with a subunit mass of 27 kDa. PfTIM WT and WT* elute at exactly this position under similar conditions. However, at a much lower concentration of 5 CM the gel filtration profile for the Y74W* mutant clearly shows two distinct species eluting at 13.9 ml and 15.3 ml. The later elution volume corresponds to the expected position for a monomeric protein with a mass of 27-28 kDa. tpi-1 3 TIM 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q07412:p.Tyr74Trp mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y W Tue Jul 12 10:21:18 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 18:42:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr74trp' Tue Jun 30 19:43:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr74Trp' Q07412:p.Trp11Phe mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W F Tue Jul 12 10:57:28 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:40:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp11phe' Tue Jun 30 17:22:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp11Phe' Q07412:p.Trp168Phe mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W F Tue Jul 12 10:21:15 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 19:02:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp168phe' Tue Jun 30 17:25:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp168Phe' Stoichiometry: 2.0 direct interaction direct interaction F5 mint Further evidence for dimer dissociation in the Y74W* mutant can be obtained by examining the concentration dependence of the collisional quenching constant, obtained from Stern-Volmer plots (Figure 5) for the quencher acrylamide [30]. The effect of addition of acrylamide over the concentration range 100 mM to 1 M was studied for protein concentrations ranging from 5 CM to 40 CM. In the case of the wild type protein (PfTIM WT) there is a very little concentration dependence of the quenching curves. In contrast, the observed quenching for the Y74W* mutant shows a pronounced concentration dependence, with a much greater degree of quenching at lower protein concentration. tpi-1 2 TIM 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q07412:p.Tyr74Trp mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y W Tue Jul 12 10:20:03 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 17:26:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr74trp' Tue Jun 30 16:54:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr74Trp' Q07412:p.Trp168Phe mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W F Tue Jul 12 10:21:54 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 15:04:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp168phe' Tue Jun 30 18:26:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp168Phe' Q07412:p.Trp11Phe mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W F Tue Jul 12 10:21:55 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 17:30:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp11phe' Tue Jun 30 17:24:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp11Phe' Stoichiometry: 2.0 direct interaction direct interaction T3 mint Table 3 provides a comparison of the denaturation parameters of PfTIM wild type and the Y74W* triple mutant. For comparison the measured parameters for the double mutant W11F/W168F and previously studied mutants are also summarized. It is immediately evident that the Y74W* mutant is considerably less stable in the presence of denaturants like Gdmcl and is also thermally more labile. tpi-1 2 TIM 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Q07412:p.Tyr74Gly mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y G Tue Jul 12 10:57:49 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 17:30:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr74gly' Tue Jun 30 16:53:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr74Gly' direct interaction direct interaction T3 mint Table 3 provides a comparison of the denaturation parameters of PfTIM wild type and the Y74W* triple mutant. For comparison the measured parameters for the double mutant W11F/W168F and previously studied mutants are also summarized. It is immediately evident that the Y74W* mutant is considerably less stable in the presence of denaturants like Gdmcl and is also thermally more labile.