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 http://mint.bio.uniroma2.it/mint lee-2012b-1 Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. 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. FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation lee-2012b-3 Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. 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. FEBS Lett. (0014-5793) 2012 Only protein-protein interactions imex curation lee-2012b-2 Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution. 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. 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 hslo-1 1252997 hsp33 HSP33 1253000 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false mint sf1b sf1d hslo-hslo 1252997 hsp33 HSP33 1253000 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified hsp33 HSP33 1253000 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false mint sf1b sf1e hslo-hslo-1 1252998 hsp33 HSP33 1253000 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified hsp33 HSP33 1253000 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false mint f3 t1 hslo-1 1252998 hsp33 HSP33 1253000 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false mint f3 t1 hslo-1 1252999 hsp33 HSP33 1253000 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 false redox-switch domain Stoichiometry: 2.0 direct interaction direct interaction false false false f2 mint