Home > Publications database > Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique > print |
001 | 1025609 | ||
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024 | 7 | _ | |a 10.1007/s40203-024-00198-0 |2 doi |
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100 | 1 | _ | |a Sanyasi, Chandrasekar |0 P:(DE-HGF)0 |b 0 |
245 | _ | _ | |a Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique |
260 | _ | _ | |a Heidelberg [u.a.] |c 2024 |b SpringerOpen |
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336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
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 |0 P:(DE-HGF)0 |b 1 |
700 | 1 | _ | |a Chinnasamy, Thirunavukkarasu |0 P:(DE-HGF)0 |b 2 |
700 | 1 | _ | |a Venugopalan, Nagarajan |0 P:(DE-HGF)0 |b 3 |
700 | 1 | _ | |a Kandavelu, Palani |0 P:(DE-HGF)0 |b 4 |
700 | 1 | _ | |a Batra-Safferling, Renu |0 P:(DE-Juel1)131950 |b 5 |u fzj |
700 | 1 | _ | |a Muthuvel, Suresh Kumar |0 P:(DE-HGF)0 |b 6 |e Corresponding author |
773 | _ | _ | |a 10.1007/s40203-024-00198-0 |g Vol. 12, no. 1, p. 23 |0 PERI:(DE-600)2702993-1 |n 1 |p 23 |t In Silico Pharmacology |v 12 |y 2024 |x 2193-9616 |
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