2012
DOI: 10.1016/j.colsurfb.2012.02.017
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Study on effect of lipophilic curcumin on sub-domain IIA site of human serum albumin during unfolded and refolded states: A synchronous fluorescence spectroscopic study

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Cited by 73 publications
(44 citation statements)
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“…Phe is not excited in most cases, and its quantum yield in protein is rather low, so the emission from this residue can be ignored [54]. Synchronous fluorescence spectra store good information while analyzing protein/agent systems by applying various Dk [55]. When Dk values between excitation and emission wavelength are stabilized at 20 or 60 nm, synchronous fluorescence can provide the characteristic information about Tyr and Trp residues of BSA, respectively [48,56].…”
Section: Resultsmentioning
confidence: 97%
“…Phe is not excited in most cases, and its quantum yield in protein is rather low, so the emission from this residue can be ignored [54]. Synchronous fluorescence spectra store good information while analyzing protein/agent systems by applying various Dk [55]. When Dk values between excitation and emission wavelength are stabilized at 20 or 60 nm, synchronous fluorescence can provide the characteristic information about Tyr and Trp residues of BSA, respectively [48,56].…”
Section: Resultsmentioning
confidence: 97%
“…2C) and 450 nm were similar with a maximum centered at $540 nm, the $10 nm blue shi of emission maximum of NCs compared to CU in water at these excitation wavelengths is due to the change in local environment and solvent. 9,[33][34][35] However, the emission spectrum for NCs obtained at l ex ¼ 355 nm (Fig. 2D) is largely different with a maximum at $536 nm and an additional new peak at a lower wavelength.…”
mentioning
confidence: 96%
“…The chemical denaturation of BSA using urea and urea-baicalein system caused a gradual decrease in the intrinsic fluorescence intensity ( Fig. 7 ) of BSA with a red shift of 7 nm in each of the cases, which resembles the fluorescence emission spectra of l -tryptophan in aqueous buffer system [63] . The denaturation of BSA caused the exposure of the buried tryptophan (Trp 213) to a more polar environment.…”
Section: Resultsmentioning
confidence: 68%