Characterization of molten globule state of fetuin at low pH

Characterization of the interaction between human lactoferrin and lomefloxacin at physiological condition: Multi-spectroscopic and modeling description

“…The biomolecular quenching rate constant was obtained from K SV , k Q ¼2.54 Â 10 12 L mol À 1 s À 1 . It can be seen that k Q is largely higher than the limiting diffusion constant K dif of the biomolecule (K dif ¼2.0 Â 10 10 L mol À 1 s À 1 ) [42,43], which suggested that the fluorescence quenching was caused mainly arisen from static quenching by complex formation [44,45]. At higher drug concentrations, the deviation from the linearity of the Stern-Volmer plot indicated that both dynamic and static quenching was involved as discussed in the literature [44,45].…”

“…The first region involves a decrease in fluorescence induced by drug binding at LMF/Hlf mole ratios up to 0.98 with a linear form. This decrease is quite important which might denote an structural modification of Hlf in such a way that tryptophan residues of Hlf located in a more hydrophilic environment [42,43]. Linear Stern-Volmer plot may either reveal the occurrence of just binding site for quencher in the proximity of the fluorophore, or indicate the existence of a single type quenching.…”

pH-Dependent Differential Interacting Mechanisms of Sodium Dodecyl Sulfate with Bovine Serum Fetuin: A Biophysical Insight

“…It may be due to the fact that at pH 2, the protein exists in a partially unfolded form with exposed hydrophobic patches and positively charge residues. 35 These charged residues exert the electrostatic repulsion between protein molecules and thus prevent aggregation. But when SDS interacts with BSF through its negatively charged head groups, then the hydrophobic tails of SDS on the protein−SDS complex become free.…”

Characterization of Acid-Induced Partially Folded Conformation Resembling a Molten Globule State of Polygalacturonase from a Filamentous Fungus Tetracoccosporium sp.

“…The MG state may have some features of the native fold. However, this state differs from native state by the absence of close packing throughout the molecule and by a substantial increase in fluctuation in side chains as well as larger parts of the molecule [3][4][5]. This folding intermediate state [6] has been demonstrated to be both as an equilibrium state under mild denaturing conditions [3] and as a kinetic intermediate of protein folding [4,7].…”

“…Fluorescence emission spectra of PG at pH 1.0-10 (1-10), b far-UV CD spectra of PG at pH 1.0-9.0 (1-9), c near-UV CD spectra of PG at pH 1 and pH 4.3, d fluorescence spectra of 30 μM ANS in the presence of PG at pH 1.0-11(1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11) …”