Interdependence of two fluorescence lifetime components τ1 and τ2 of wild-type BCA II (■ WT) and its two mutant forms ( L139A and A53C-A76C). Each point was obtained by fitting fluorescence decay curves of protein solution at definite urea concentration. Thick color lines show the “unfolding pathway” for each protein with increase in urea concentration from 0 to 7.5 M. The relative deviations for τ1 and τ2 were ≤3% and ≤7% correspondingly.</p
<p>(A) Urea induced unfolding transition curves of BL at pH 7.4 (-▪-) and pH 2.0 (–▴–) monitored thr...
<p>A) Protein samples were incubated at 50°C with different concentrations of urea from 4 M to 8 M f...
<p>(A) Heat-induced unfolding monitored by measuring the CD signal at 222 nm; after unfolding, the C...
Interdependence of fluorescence intensities at 320 and 360 nm for wild-type BCA II (■ WT) and its tw...
Dependence of fluorescence lifetimes τ1 (A) and τ2 (B) on urea concentration of wild-type BCA II (■ ...
Dependence of fluorescence lifetimes τ1 (A) and τ2 (B) on urea concentration of wild-type BCA II (■ ...
Dependence of fluorescence intensity I at 360 nm (A) and 320 nm (B) on urea concentration for wild-t...
Dependence of fluorescence lifetimes τ1 (A) and τ2 (B) on urea concentration of wild-type BCA II (■ ...
<p>Changes in average emission wavelength (AEW) of tryptophan fluorescence are represented as a func...
<p><b>(A, B)</b> Tryptophan fluorescence spectra of association domain (A) and its mutant (F394L/I41...
<p>The urea-induced unfolding profile of BSA and BBE-BSA complex at BBE/BSA molar ratios of 0∶1 and ...
<p>Evolution of the fluorescence emission (integrated intensity) as a function of urea concentration...
<p>(A) Emission spectra of the protein in 0–7.5 M urea were recorded as in <a href="http://www.ploso...
<p>(a) The black symbols represented fluorescence (327 nm) and red symbols circular dichroismn (222 ...
<p>Unfolding/refolding transitions were recorded starting with initially folded (0.6 M urea, filled ...
<p>(A) Urea induced unfolding transition curves of BL at pH 7.4 (-▪-) and pH 2.0 (–▴–) monitored thr...
<p>A) Protein samples were incubated at 50°C with different concentrations of urea from 4 M to 8 M f...
<p>(A) Heat-induced unfolding monitored by measuring the CD signal at 222 nm; after unfolding, the C...
Interdependence of fluorescence intensities at 320 and 360 nm for wild-type BCA II (■ WT) and its tw...
Dependence of fluorescence lifetimes τ1 (A) and τ2 (B) on urea concentration of wild-type BCA II (■ ...
Dependence of fluorescence lifetimes τ1 (A) and τ2 (B) on urea concentration of wild-type BCA II (■ ...
Dependence of fluorescence intensity I at 360 nm (A) and 320 nm (B) on urea concentration for wild-t...
Dependence of fluorescence lifetimes τ1 (A) and τ2 (B) on urea concentration of wild-type BCA II (■ ...
<p>Changes in average emission wavelength (AEW) of tryptophan fluorescence are represented as a func...
<p><b>(A, B)</b> Tryptophan fluorescence spectra of association domain (A) and its mutant (F394L/I41...
<p>The urea-induced unfolding profile of BSA and BBE-BSA complex at BBE/BSA molar ratios of 0∶1 and ...
<p>Evolution of the fluorescence emission (integrated intensity) as a function of urea concentration...
<p>(A) Emission spectra of the protein in 0–7.5 M urea were recorded as in <a href="http://www.ploso...
<p>(a) The black symbols represented fluorescence (327 nm) and red symbols circular dichroismn (222 ...
<p>Unfolding/refolding transitions were recorded starting with initially folded (0.6 M urea, filled ...
<p>(A) Urea induced unfolding transition curves of BL at pH 7.4 (-▪-) and pH 2.0 (–▴–) monitored thr...
<p>A) Protein samples were incubated at 50°C with different concentrations of urea from 4 M to 8 M f...
<p>(A) Heat-induced unfolding monitored by measuring the CD signal at 222 nm; after unfolding, the C...