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<p>Page créée avec « Figure 5 Overlapping of fluorescence spectra of HAase (CHAase = 2.0 �� 10?6?mol?L?1) with absorption spectra of liquiritigenin (Cliquiritigenin = 2.0 �� 10?6?mol?L... »</p> <p><b>Nouvelle page</b></p><div>Figure 5 Overlapping of fluorescence spectra of HAase (CHAase = 2.0 �� 10?6?mol?L?1) with absorption spectra of liquiritigenin (Cliquiritigenin = 2.0 �� 10?6?mol?L?1). In the present case, K2 = 2/3, n = 1.366, and �� = 0.118 [21]. According to (6)�C(8), the values of the parameters were calculated to be J = 1.899 �� 10?14?cm3?moL?1?L, E = 0.07, R0 = 3.23?nm, and r = 5.04?nm. The distance between liquiritigenin and HAase was obviously less than 7?nm and 0.5R0 [http://en.wikipedia.org/wiki/SERCA SERCA] Conformational Investigations In order to understand the possible effect of liquiritigenin binding on the secondary structure of HAase, the synchronous fluorescence and the three-dimensional fluorescence spectra were measured in the absence and presence of liquiritigenin. When the wavelength interval (����) between the excitation and emission wavelength is stabilized at 15 or 60?nm, the synchronous fluorescence gives characteristic information of tyrosine (Tyr) residues or tryptophan (Trp) residues, respectively [22, 23]. The synchronous [http://www.selleckchem.com/products/BI6727-Volasertib.html click here] fluorescence spectra at these two different wavelength intervals are presented in Figure 6. As the concentration of liquiritigenin increased gradually, the synchronous fluorescence intensity decreased; however, an obvious shift of the Tyr peak and Trp peak cannot be observed in Figures 6(a) and 6(b), which indicated that liquiritigenin has a weak effect on the microenvironment of Tyr and Trp residues in HAase. On the other hand, it can be seen from Figure 7 that the slope was higher when ���� was 60?nm, which indicated that liquiritigenin was closer to the Trp residues than to the Tyr residues and the microenvironments of Trp residues were influenced more [http://www.selleckchem.com/products/NVP-AUY922.html Luminespib] than those of Tyr residues. Figure 6 Synchronous fluorescence spectra of interaction between HAase and liquiritigenin at (a) ���� = 15?nm and (b) ���� = 60?nm at room temperature. Peak from up to down Cliquiritigenin = (0, 4.0, 8.0, 12.0, 16.0,20.0, ... Figure 7 The quenching of HAase synchronous fluorescence by liquiritigenin. CHAase = 2.0 �� 10?6?mol?L?1, (��) ���� = 15?nm and (��) ���� = 60?nm (n = 3). Three-dimensional fluorescence spectroscopy is a powerful method for providing conformational and structural information of proteins [24]. The three-dimensional fluorescence spectra of HAase and liquiritigenin-HAase systems are shown in Figure 8. It can be seen from Figure 8(a) that the three-dimensional fluorescence contour spectrum of HAase shows contour maxims at ��ex/��em = 278/330?nm arising by ��-��? transition of aromatic amino acids in HAase. In Figure 8(b), the HAase fluorescence peak shifted to 278/335?nm.</div>

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