Biology subjects

Kwon, T. H.

Publications and source records attributed to Kwon, T. H..

2 recordsLinked to original sources

bioRxiv2023

Purification, crystallization, and preliminary structural analysis of multivalent immunogenic effector protein-anchored SARS-CoV-2 RBD

The continuous spread of highly transmissible variants of concern and the potential diminished effectiveness of existing vaccines necessitate ongoing research and development of new vaccines. Immunogenic molecule-anchored antigen has demonstrated superior efficacy in subunit vaccination, primarily due to enhanced cellular uptake facilitated by the affinity between the surface of Immunogenic molecule and the cell membrane. Based on the Immunogenic recombinase B. malayi RecA (BmRecA), we have overexpressed the construct of BmRecA with SARS-CoV-2 RBD (BmRecA-RBD) that exists as a stable helical filament formation; it was purified and crystallized to obtain X-ray diffraction data at 2.7 [A], belonged to the hexagonal symmetry group P65 in the unit-cell parameters of a=b=122.12, c=75.55 and ={beta}=90{degrees}, {gamma}=120{degrees}. The Matthews coefficient was estimated to be 3.12 [A]3 Da-1, corresponding to solvent contents of 52.65.

biophysics↗

bioRxiv2022

Yeast nicotinate-nucleotide pyrophosphorylase in complex with its ligand: Crystallization and Preliminary structural approaches

Pyridine-2,3-dicarboxylic acid which is a biologically potent molecule implicated in neurodegenerative environment is catalyzed by nicotinate-nucleotide pyrophosphorylase (NMnPP) to produce a precursor molecule, nicotinate mononucleotide (NMn), of de novo biosynthesis of the coenzyme nicotinamide adenine dinucleotide (NAD+). The protein preparation, crystallization, and preliminary structural features of full-length enzyme in complex with product reactant suggest that yeast NMnPP acts as stable hexamer formation. S. cerevisiae NMnPP was obtained and diffracted to a resolution of 1.74 [A] and 1.99 [A] for apo and complex forms, belonged to the trigonal symmetry group R32 in the unit-cell parameters of a=b=155.313, c=67.507 and a=b=155.091, c=69.204, respectively. Based on our comparison of eukaryotic NMnPP structures in the apo and complex forms, we propose functional and structural investigation for the product binding and hexamer stabilization.

biophysics↗