Journal: bioRxiv
Article Title: Leptospira interrogans triosephosphate isomerase: exploring the structural determinants of stability, high reaction rate and specificity
doi: 10.1101/2020.12.04.412312
Figure Lengend Snippet: Purification and characterization of Leptospira interrogans TIM (LiTIM). ( A ) 12% SDS-PAGE showing the final purified protein used for further characterisation. ( B ) Far-UV CD spectrum and ( C ) tryptophan intrinsic fluorescence spectrum of the purified protein confirm a well folded form in solution. ( D ) Crystals obtained for the apo form of LiTIM. The crystal in the lower panel was soaked with substrate to obtain the holo form of the protein. ( E ) Analytical gel filtration chramatography indicates that it is a dimer in the solution (PfTIM WT, known to be dimeric, was used as the control ). ( F ) LiTIM protein sequence (251 residues)-catalytic residues in red bold, residues that showed conformational change upon substrate binding in bold underline, and other periferal, conserved residues that interact with substrate are shown in underlined letters. ( G ) LC-ESI/MS of the purified LiTIM protein agrees with the expected mass.
Article Snippet: Triosephosphate isomerase gene ( tim gene ID: LEP2GSC113_RS0110880) was amplified from five days old Ellinghausen-McCullough-Johnson-Harris (EMJH) culture of Leptospira interrogans (Li) serovar Icterohaemorrhagiae strain RGA (Regional Medical Research Centre, Indian Council for Medical Research, Port Blair, India; ATCC: 23581.
Techniques: Purification, SDS Page, Fluorescence, Filtration, Control, Sequencing, Binding Assay
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