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Rachana Tomar, Dushyant K. Garg, Rahul Mishra, Ashwani K. Thakur and Bishwajit Kundu N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone FEBS Journal 280

Article first published online: 29 APR 2013 | DOI: 10.1111/febs.12271

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N-terminal domain of Pyrococcus furiosus l-asparaginase forms stable, polydispersed oligomers. It helps in folding of the C-terminal domain and prevents thermal and refolding-mediated aggregation of a variety of substrate proteins, thus acting as molecular chaperone. It also inhibits polyQ and Aβ amyloidogenesis. It may be used in aggregation prevention in heterologous expression systems and also in therapeutic intervention of amyloidogenesis.

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