Related Experiment Video
Updated: May 18, 2026

Online Size-exclusion and Ion-exchange Chromatography on a SAXS Beamline
Published on: January 5, 2017
Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS
Chandrasekar Sanyasi1, Susmida Seni Balakrishnan1, Thirunavukkarasu Chinnasamy2
1Department of Bioinformatics, School of Life Sciences, Pondicherry University, Pondicherry, 605014 India.
Abstract:
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.
Supplementary Information:
The online version contains supplementary material available at 10.1007/s40203-024-00198-0.

