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The research article investigates the interactions of synthesized zinc(II) complexes with globular proteins and free tryptophan using fluorescence spectroscopy. The study reveals that the binding affinity of these complexes varies significantly based on their structural features, with planar aromatic complexes showing the strongest interactions. Thermodynamic analysis indicates that the binding process is spontaneous and favorable, with binding strength decreasing at higher temperatures.

Author

17139116

Language

EN