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001025609 1001_ $$0P:(DE-HGF)0$$aSanyasi, Chandrasekar$$b0
001025609 245__ $$aInsights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique
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001025609 520__ $$aThe dynamic behavior of Protein Disulfide Isomerase (PDI) in an aqueous solution environment under physiologically active pH has been experimentally verified in this study using Small Angle X-ray Scattering (SAXS) technique. The structural mechanism of dimerization for full-length PDI molecules and co-complex with two renowned substrates has been comprehensively discussed. The structure models obtained from the SAXS data of PDI purified from bovine liver display behavior duality between unaccompanied-enzyme and after engaged with substrates. The analysis of SAXS data revealed that PDI exists as a homo-dimer in the solution environment, and substrate induction provoked its segregation into monomer to enable the enzyme to interact systematically with incoming clients.
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001025609 7001_ $$0P:(DE-HGF)0$$aBalakrishnan, Susmida Seni$$b1
001025609 7001_ $$0P:(DE-HGF)0$$aChinnasamy, Thirunavukkarasu$$b2
001025609 7001_ $$0P:(DE-HGF)0$$aVenugopalan, Nagarajan$$b3
001025609 7001_ $$0P:(DE-HGF)0$$aKandavelu, Palani$$b4
001025609 7001_ $$0P:(DE-Juel1)131950$$aBatra-Safferling, Renu$$b5$$ufzj
001025609 7001_ $$0P:(DE-HGF)0$$aMuthuvel, Suresh Kumar$$b6$$eCorresponding author
001025609 773__ $$0PERI:(DE-600)2702993-1$$a10.1007/s40203-024-00198-0$$gVol. 12, no. 1, p. 23$$n1$$p23$$tIn Silico Pharmacology$$v12$$x2193-9616$$y2024
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