Two distinct intermediates of trigger factor are populated during guanidine denaturation

Effects of glutathione on amyloid fibrillation of hen egg-white lysozyme

“…ANS, a hydrophobic, aromatic and charged fluorescent probe, is widely used in studying the molten globule intermediate state (partially folded state) in protein folding experiments [34,35]. It is also used to determine the binding sites of proteins [36,37], and detecting exposed nonpolar surfaces in protein solutions [38][39][40]. The preferential binding of ANS to hydrophobic clusters gives rise to an enhancement in fluorescence emission that accompanies a blue shift of the emission maxima and a dramatic increase in quantum yield [35,38,40].…”

“…It is also used to determine the binding sites of proteins [36,37], and detecting exposed nonpolar surfaces in protein solutions [38][39][40]. The preferential binding of ANS to hydrophobic clusters gives rise to an enhancement in fluorescence emission that accompanies a blue shift of the emission maxima and a dramatic increase in quantum yield [35,38,40]. As a matter of fact, ANS has been employed to indirectly probe for the information of surface hydrophobicity in a significant body of research associated with the formation of amyloid fibrils induced by acidic pH [41][42][43].…”

Effect of curcumin on the amyloid fibrillogenesis of hen egg-white lysozyme

“…The fluorescent hydrophobic dye ANS is commonly utilized to demonstrate the presence of partially folded conformations of globular proteins and probe for conformational properties and solvent exposure of the hydrophobic surfaces in proteins [26][27][28]. The preferential binding of ANS to hydrophobic clusters gives rise to an enhancement in fluorescence emission accompanying a blue shift of the spectral maximum [26,27,29].…”

Fibril Formation of Bovine α-Lactalbumin Is Inhibited by Glutathione

“…36 It is also used to determine the binding sites of proteins, 37 and detect exposed nonpolar surfaces in protein solutions. 38 The preferential binding of ANS to hydrophobic clusters leads to an enhancement in fluorescence emission that accompanies a blue shift of the emission maxima and a dramatic increase in quantum yield. 38 As illustrated in Figure 4a, the ANS fluorescence intensity (or surface hydrophobicity) of fresh α-LA with or without GSH was found to be low (~297-337 A.U.)…”

“…38 The preferential binding of ANS to hydrophobic clusters leads to an enhancement in fluorescence emission that accompanies a blue shift of the emission maxima and a dramatic increase in quantum yield. 38 As illustrated in Figure 4a, the ANS fluorescence intensity (or surface hydrophobicity) of fresh α-LA with or without GSH was found to be low (~297-337 A.U.) due to the fact that the hydrophobic site groups are hidden inside the native protein with compact and folded structure.…”