%0 Journal Article
%A Sanyasi, Chandrasekar
%A Balakrishnan, Susmida Seni
%A Chinnasamy, Thirunavukkarasu
%A Venugopalan, Nagarajan
%A Kandavelu, Palani
%A Batra-Safferling, Renu
%A Muthuvel, Suresh Kumar
%T Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique
%J In Silico Pharmacology
%V 12
%N 1
%@ 2193-9616
%C Heidelberg [u.a.]
%I SpringerOpen
%M FZJ-2024-03003
%P 23
%D 2024
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%R 10.1007/s40203-024-00198-0
%U https://juser.fz-juelich.de/record/1025609