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 Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. FEBS Lett. (0014-5793) 2012 imex curation Lee YS., Ryu KS., Kim SJ., Ko HS., Sim DW., Jeon YH., Kim EH., Choi WS., Won HS. suggested by lperfetto Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Lee YS., Ryu KS., Kim SJ., Ko HS., Sim DW., Jeon YH., Kim EH., Choi WS., Won HS. suggested by lperfetto FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. FEBS Lett. (0014-5793) 2012 imex curation Lee YS., Ryu KS., Kim SJ., Ko HS., Sim DW., Jeon YH., Kim EH., Choi WS., Won HS. suggested by lperfetto 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 Lee YS., Ryu KS., Kim SJ., Ko HS., Sim DW., Jeon YH., Kim EH., Choi WS., Won HS. suggested by lperfetto FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. FEBS Lett. (0014-5793) 2012 imex curation Lee YS., Ryu KS., Kim SJ., Ko HS., Sim DW., Jeon YH., Kim EH., Choi WS., Won HS. suggested by lperfetto Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Lee YS., Ryu KS., Kim SJ., Ko HS., Sim DW., Jeon YH., Kim EH., Choi WS., Won HS. suggested by lperfetto FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation hslo_ecoli 33 kDa chaperonin yrfI Heat shock protein 33 hslO b3401 JW5692 protein protein ecoli Escherichia coli (strain K12) MPQHDQLHRYLFENFAVRGELVTVSETLQQILENHDYPQPVKNVLAELLVATSLLTATLKFDGDITVQLQGDGPMNLAVINGNNNQQMRGVARVQGEIPENADLKTLVGNGYVVITITPSEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGDVDGKPAAGGMLLQVMPAQNAQQDDFDHLATLTETIKTEELLTLPANEVLWRLYHEEEVTVYDPQDVEFKCTCSRERCADALKTLPDEEVDSILAEDGEIDMHCDYCGNHYLFNAMDIAEIRNNASPADPQVH 18F05BD2F0257552 hslo-1 2 HSP33 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 mint sf1b sf1d In the gel-filtration analysis (Suppl. Fig. 1), our reduced Hsp33 (RedHsp33M) had an apparent molecular weight (Mapp) of approximately 38 kDa, indicative of a monomeric state in solution. In contrast, the oxidized Hsp33 solution exhibited three distinct peaks in its elution profile. The first peak (Mapp > 90 kDa) and the middle peak (Mapp ≈ 72 kDa) could be assigned to oligomeric (OxHsp33Oli) and dimeric Hsp33 (OxHsp33Di), respectively. hslo-hslo 2 HSP33 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified HSP33 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint In the gel-filtration analysis (Suppl. Fig. 1), our reduced Hsp33 (RedHsp33M) had an apparent molecular weight (Mapp) of approximately 38 kDa, indicative of a monomeric state in solution. In contrast, the oxidized Hsp33 solution exhibited three distinct peaks in its elution profile. The first peak (Mapp > 90 kDa) and the middle peak (Mapp ≈ 72 kDa) could be assigned to oligomeric (OxHsp33Oli) and dimeric Hsp33 (OxHsp33Di), respectively. sf1b sf1e hslo-1 3 HSP33 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain redox-switch domain Stoichiometry: 2.0 direct interaction direct interaction f2 mint hslo-hslo-1 1 HSP33 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified HSP33 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint Thus, we investigated the tryptophanyl environment, by fluorescence spectroscopy (Fig. 3 and Table 1) in order to assess the linker domain structure in solution. This conclusion clarifies that the change does not occur in the oxidized monomer and is attributed to dimerization and oligomerization. f3 t1 hslo-1 1 HSP33 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 mint Thus, we investigated the tryptophanyl environment, by fluorescence spectroscopy (Fig. 3 and Table 1) in order to assess the linker domain structure in solution. This conclusion clarifies that the change does not occur in the oxidized monomer and is attributed to dimerization and oligomerization. f3 t1