the 3D dimeric structure of BADH2 is modeled using homology modeling. Each monomer comprises of 3 domains (substrate-binding, NAD+-binding, and oligomerization domains). The NAD+-binding domain is the most mobile. A scissor-like motion is observed between the monomers. Key inter-subunit salt bridges contributing to dimerization are identified. E487, D491, E492, K498, and K502 form strong salt bridges with charged residues on the adjacent monomer. Specifically, the nearly permanent R430-E487 hydrogen bond (over 90%) highlights its key role in dimer association
enzyme secondary structrue analysis, pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+, overview. pkBADH shows 17% of unordered structure, 41% of alpha-helix, and 29% of beta-sheet
enzyme secondary structrue analysis, pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+, overview. pkBADH shows 17% of unordered structure, 41% of alpha-helix, and 29% of beta-sheet
secondary and tertiary structure of pkBADH in presence or absence of NAD+, fluorescence quenching spectra of pkBADH titrated with variable NAD+ concentrations in presence of potassium, overview. The deconvolution data analysis shows a 13% increase in the pkBADH helical structure, a decrease of 7% in beta-sheet content and 6% in turns content during the pkBADH-NAD+ complex formation