2009
DOI: 10.1016/j.ejmech.2009.04.047
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Fluorescence spectroscopic investigation of the interaction between chloramphenicol and lysozyme

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Cited by 98 publications
(43 citation statements)
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“…Obviously, 'r' was smaller than 7 nm, which was in accordance with the Foster's non-radiative energy transfer theory, suggesting the energy transfer from LYSO to TiO 2 nanoparticles occurs with high probability. This accorded with conditions of Forster's theory and indicated again a static quenching between lysozyme and TiO 2 NPs [63,69].…”
Section: Energy Transfer From Lyso To Tio 2 Nanoparticlessupporting
confidence: 84%
See 1 more Smart Citation
“…Obviously, 'r' was smaller than 7 nm, which was in accordance with the Foster's non-radiative energy transfer theory, suggesting the energy transfer from LYSO to TiO 2 nanoparticles occurs with high probability. This accorded with conditions of Forster's theory and indicated again a static quenching between lysozyme and TiO 2 NPs [63,69].…”
Section: Energy Transfer From Lyso To Tio 2 Nanoparticlessupporting
confidence: 84%
“…In contrast, an obvious red shift is observed for tryptophan residues with increasing concentration of TiO 2 NPs; it expresses that the conformation of tryptophan micro-region was changed. Many researchers reported the similar type of conformational changes [62,[68][69][70][71][72].…”
Section: Characteristics Of Synchronous Fluorescence Spectramentioning
confidence: 94%
“…As shown in Fig. 5, the Stern-Volmer plots show that the Stern-Volmer quenching constant (the slope, k sv ) decreases with increasing temperature; and the values of k q (1.6 9 10 13 l mol -1 s -1 and 9.7 9 10 12 l mol -1 s -1 at 298 and 310 K, respectively) are much greater than 2.0 9 10 10 l mol -1 s -1 , indicating that the quenching mechanism of PTP1B by complex 1 is not initiated by dynamic collision but by static quenching interactions, i.e., the formation of complex between 1 and PTP1B (Guo et al 1996;Ding et al 2009). For static quenching interactions, the cumulative binding constant is calculated from the following Eq.…”
Section: Ptp Inhibition Studiesmentioning
confidence: 94%
“…The calculated value of k q (2.05 × 10 14 M − 1 s − 1 at 298 K) from Stern-Volmer plots (see Fig. S12, Appendix A) was much greater than 2.0 × 10 10 M − 1 s − 1 , indicating that the quenching mechanism of PTP1B by complex 1 was not initiated by dynamic collision but by static quenching interaction [15,20,52,53]. For static quenching interaction, the number of binding sites (n) could be obtained from the regression curve based on the following Eq.…”
Section: Fluorescence Study On the Interaction Between Ptp1b And Compmentioning
confidence: 96%