Investigation of neohesperidin dihydrochalcone binding to human serum albumin by spectroscopic methods

Conformational alterations induced by novel green 16-E2-16 gemini surfactant in xanthine oxidase: Biophysical insights from tensiometry, spectroscopy, microscopy and molecular modeling

“…quite evident, hence, we can conclude that the quenching proceeds via static pathway; and this observation is in complement with fluorescence prediction. Similar results have been obtained for protein-drug, protein-herbicide and protein-flavonoid interactions [62][63][64][65].…”

Safeguarding the catalytic activity and stability of polyaniline chitosan silver nanocomposite bound beta-galactosidase against product inhibitors and structurally related compound

“…Fluorescence spectroscopy is one of the most excellent techniques to investigate the binding of bioactive molecules to proteins as it is more sensitive compared to other optical methods [34,35]. Three amino acid residues; viz, tryptophan (Trp), tyrosine (Tyr) and phenylalanine (Phe) are primarily responsible for the intrinsic fluorescence of bGS.…”

Binding characteristics of psoralen with trypsin: Insights from spectroscopic and molecular modeling studies

“…These well-mixed solutions were stood for 5 min to equilibrate, then the fluorescence spectra were measured in the wavelength range of 300-500 nm upon an excitation at 280 nm. For eliminating the possibility of inner filter effect and re-absorption arising from UV absorption, the fluorescence data were corrected for absorption of excitation light and emitted light according to the following equation [18]:…”