2000
DOI: 10.1016/s0301-4622(00)00210-6
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Phase-fluorimetry study on dielectric relaxation of human serum albumin

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Cited by 15 publications
(14 citation statements)
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“…The data of the time-resolved fluorescent spectroscopy of HSA revealed several relaxation components, which are attributed to either motions of the protein in the vicinity of chromophore or the dynamics of its hydration shell. The phase-fluorimetry of dielectric relaxations in HSA revealed two relaxation components in the regions of 0.4-2.0 ns and 4.9-8.1 ns [10], which correspond to our components τ 6 and τ 7 . Time-resolved spectroscopy of the single tryptophan residue W214 in HSA revealed relaxation times of 25-100 ps [13].…”
Section: Introductionsupporting
confidence: 58%
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“…The data of the time-resolved fluorescent spectroscopy of HSA revealed several relaxation components, which are attributed to either motions of the protein in the vicinity of chromophore or the dynamics of its hydration shell. The phase-fluorimetry of dielectric relaxations in HSA revealed two relaxation components in the regions of 0.4-2.0 ns and 4.9-8.1 ns [10], which correspond to our components τ 6 and τ 7 . Time-resolved spectroscopy of the single tryptophan residue W214 in HSA revealed relaxation times of 25-100 ps [13].…”
Section: Introductionsupporting
confidence: 58%
“…We compared our data with the results of the broadband acoustic spectroscopy [8,9] and optical spectroscopy of the HSA [10][11][12][13]. Four major components were detected in the acoustic spectra of HSA in various experimental conditions [9].…”
Section: Introductionmentioning
confidence: 96%
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“…respectively. Such changes in emission peak of W214 in native protein is reported to be due to the solvent relaxation process [66]. Drawing analogy with the native protein, the observed dynamic Stokes' shift for fibrillar solution is also assigned to the solvent relaxation process.…”
Section: Steady-state Emission Measurementsmentioning
confidence: 78%
“…Solvatochromic organic dyes were primarily introduced as "polarity probes" [18,24] based on their strong polarity-dependent shifts of fluorescence spectra, and the sensitivity of their response to other factors, such as intermolecular hydrogen bonding, electric fields produced by the charged groups and adsorbed ions or the extent of dielectric relaxations was simply ignored. The importance of the latter factor has become apparent with the introduction of analysis of spectral shifts based on time-resolved spectroscopy [17,21,28,29] and on the observation of Red-Edge effects [19][20][21]30,31]. Regarding the other factors, it is the spectroscopic properties of the probes, which limit their evaluation.…”
Section: Introductionmentioning
confidence: 99%