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This result is consistent with published findings that dimeric Prx1 exhibits significant peroxidase activity, while the decameric form acts as a chaperone with decreased peroxidase activity [ 36, 37].
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The HDM activity increases while the HDS activity decreases with increasing average pore diameter.
The higher molecular weight complex shows chaperone function, the dimeric form mostly functions as a peroxidase, whereas the decameric form shows both these activities [ 37].
Complex formation leads to disassembly of the decameric form of Prx1, which is known to increase its peroxidase activity.
The decameric structure of PTX3, particularly its disulphide bonded structure, is thought to underpin this activity [ 31, 43].
In agreement, incubation of the decameric Prx1 with the p66CH2CB Cys59Ser mutant, which lacks the redox-active cysteine residue and therefore cannot oxidize Prx1, does not result in the ladder of bands.
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To this end, we constructed a fusion protein displaying ten VHH domains per assembly, taking advantage of the decameric structure of Brucella spp. lumazine synthase [35].
The peptide molecules were found to be dynamic and reversibly associating and dissociating, eventually ending up in the decameric state as indicated by the averaged occupations over all trajectories.
Interestingly, no domain swapping is observed in the decameric structures of T. tenax FBPA or M. jannaschii ADH synthase, indicating that it is not a requirement for formation of a stable aldolase decamer.
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