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100 1 _ |a Sanyasi, Chandrasekar
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245 _ _ |a Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique
260 _ _ |a Heidelberg [u.a.]
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520 _ _ |a The 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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700 1 _ |a Balakrishnan, Susmida Seni
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700 1 _ |a Chinnasamy, Thirunavukkarasu
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700 1 _ |a Venugopalan, Nagarajan
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700 1 _ |a Kandavelu, Palani
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700 1 _ |a Batra-Safferling, Renu
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700 1 _ |a Muthuvel, Suresh Kumar
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773 _ _ |a 10.1007/s40203-024-00198-0
|g Vol. 12, no. 1, p. 23
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|t In Silico Pharmacology
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