inner-banner-bg

Insights of Herbal Medicine(IHM)

ISSN: 2834-7749 | DOI: 10.33140/IHM

Excitation-Induced Conformational Changes in ecDHFR: Attenuable Luminance Element in Instant Reaction States

Abstract

Chia Yu, Chang, Ronnie E, Thebeau and Fang Yu, Chang

Escherichia coli dihydrofolate reductase (ecDHFR) is an enzyme that synthesizes 5,6,7,8- tetrahydrofolate a kind of crucial compound involved in nucleotide biosynthesis. Recent research has shown that when ecDHFR undergoes specific reactions and subsequently exposed to excitation, it is transformed into a stable fluorescent protein. Complexes formed involving dihydrofolate, NADPH inside wild-type and mutants ecDHFR with an ionic NADPH+ and tetrahydrofolate under Arrhenius acid solutions have exhibited electronic resonance effects. These findings suggest that microscale reactions are governed by specific potential energies form bind formation, electrostatic attraction, ionic force in the hydrophobic steady state. In Computed Tomography, tracers’ move forward, the ability to generate realistic excitation response ratios and compare the wild-type and mutant ecDHFR before and after reactions will provide further insights into the dynamic protein structure workings of ecDHFR and its relationship with image formation capability under micro solution.

PDF