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 anonymous-2014w-1 The YCF54 protein is part of the membrane component of Mg-protoporphyin IX monomethyl ester cyclase from barley (Hordeum vulgare L.) in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie dbolliva@iwu.edu 2014 imex curation Bollivar D., Braumann I., Berendt K., Gough S.P., Hansson M. FEBS J. (1742-464X) Only protein-protein interactions f2d891_horvv protein protein horvd Hordeum vulgare var. distichum (Two-rowed barley) MVAPATLSLRPCATLAPSRAAHAHAGFAHTSRPALSVSCPPTRFETLRRAATAVSDRQGSAEPSEKQEDKPRTYYFLVANAKFMLDDEEHFQEQLQEKLRLYEERSKEQDFWLVIEPKFLDRFPNVAKRLKRPAVALVSTDRNWIRFMKLRLDRVLAEQFDAETVEEALASNPAELKFDKPDKWTAPYPKYESGWWEAFLPPKSSNGTA predicted protein 1530065 n/a Ycf54 1530066 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false Stoichiometry: 3.0 direct interaction direct interaction false false false f2 The recombinant Ycf54 protein was observed in several different oligomeric states when separated on gel-permeation chromatography (Fig. 2A), corresponding to approximate monomer (25 kDa; 1.2 x predicted size), trimer (57 kDa; 2.7 x predicted size) and pentamer (108 kDa; 5.1 x predicted size), though the largest molecular weight complex reported here is beyond the resolution of the chromatography column used so the predicted size of this complex should be treated with some caution. When separated on SDS-PAGE the polypeptides present in the multimeric complexes on gel permeation chromatography ran at the same size as the expressed Ycf54 polypeptide (Fig. 2B) predicted protein-1 1530065 n/a Ycf54 1530066 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false Stoichiometry: 5.0 direct interaction direct interaction false false false f2 The recombinant Ycf54 protein was observed in several different oligomeric states when separated on gel-permeation chromatography (Fig. 2A), corresponding to approximate monomer (25 kDa; 1.2 x predicted size), trimer (57 kDa; 2.7 x predicted size) and pentamer (108 kDa; 5.1 x predicted size), though the largest molecular weight complex reported here is beyond the resolution of the chromatography column used so the predicted size of this complex should be treated with some caution. When separated on SDS-PAGE the polypeptides present in the multimeric complexes on gel permeation chromatography ran at the same size as the expressed Ycf54 polypeptide (Fig. 2B)