Investigating the Electrostatic Role of a Critical Arginine for the Catalysis of E. Coli ADP-Glucose Pyrophosphorylase
نویسنده
چکیده
targeting riboflavin binding protein (RFBP), which acts as a model protein for the riboflavin receptor. By characterizing the binding interactions between riboflavin dendrimer gold nanoparticle conjugates and RFBP, the efficacy of this platform for a targeted approach of drug delivery can be predicted more accurately. Atomic Force Microscopy (AFM) was used for biological imaging studies of these riboflavin-dendrimer complexes conjugated with goldnanoparticles. using a systematic ‘‘building block’’ approach, the size distribution of riboflavin dendrimer gold nanoparticle conjugates was mapped. Changes in height upon binding to RFBP and subsequent removal by competitive binding ligands demonstrate that this method could present a novel approach to screening the binding of drugs to drug targets.
منابع مشابه
The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme.
ADP-glucose pyrophosphorylase catalyzes the first and limiting step in starch biosynthesis and is allosterically regulated by the levels of 3-phosphoglycerate and phosphate in plants. ADP-glucose pyrophosphorylases from plants are heterotetramers composed of two types of subunits (small and large). In this study, the six Arabidopsis thaliana genes coding for ADP-glucose pyrophosphorylase isofor...
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