2 * 60000, SDS-PAGE, dimerization after prolonged storage at -20°C, freeze-thawing or heating at 60°C, monomers held together by an intermolecular disulfide bond
dimerization of COA6 is unaffected by its concentration. The residues in helix 3 of COA6 are likely involved in dimerization. Dimerization is not due to inter-disulfide bonding between cysteine residues of each COA6 monomer. COA6 structure analysis, overview
dimerization of COA6 is unaffected by its concentration. The residues in helix 3 of COA6 are likely involved in dimerization. Dimerization is not due to inter-disulfide bonding between cysteine residues of each COA6 monomer. COA6 structure analysis, overview
dimerization of COA6 is unaffected by its concentration. The residues in helix 3 of COA6 are likely involved in dimerization. Dimerization is not due to inter-disulfide bonding between cysteine residues of each COA6 monomer. COA6 structure analysis, overview
2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry
2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry
the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices
the enzyme structure of MdbACm possesses two conserved features found in actinobacterial MdbA enzymes, a thioredoxin-like fold and an extended alpha-helical domain. The MdbA alpha-helical domain comprises 7 alpha-helices