<p><b>A</b>, Intrinsic protein fluorescence spectra of APC-MCR measured in 1°C steps from 20°C to 70°C, indicated by a greyscale gradient from black to light grey<b>. B</b>, Comparison of intrinsic tyrosine fluorescence spectra normalised to the maxima. Experiment and colour code as in A. C Temperature dependence of intrinsic tyrosine fluorescence emission of MCR upon stepwise increase of temperature at 340 nm (black) and 304 nm (grey) normalised on maxima of emission. </p
<p>Far-UV CD (A) and intrinsic Trp fluorescence (B) spectra of the designated proteins (bound with o...
<p>The changes are reflected by (<b>A</b>) synchronous fluorescence for tryptophan emission, (<b>B</...
a<p>(M<sup>−1</sup>s<sup>−1</sup> (×10<sup>5</sup>).</p>b<p>Melting temperature (T<sub>m</sub> in °C...
Time-resolved fluorescence spectroscopy was used to show that multiple tyrosine residues of a protei...
<p>Dark circles represent the experimental data for Wt. Gray and white symbols correspond to Lys107-...
In a case study on five homologous alpha-amylases we analyzed the properties of unfolded states as o...
<p>The protein reconstituted in detergent micelles show one principal transitions in comparison with...
The probe concentration in LUVs is 3.6%. (A), 379 nm cPyD9. (B), 373 nm cPyO3. (C), 388 nm, I3 “cons...
<p>Fluorescence scan diagrams based on <i>Sypro Orange</i> (Thermo Fisher Scientific) binding upon t...
<p>The complete scan for the spectra related to (<b>A</b>) and (<b>B</b>) are presented in <a href="...
<p>(A) Temperature as a function of time during FLIPR temperature-activation assay. (B) Representati...
<p>The fractions of unfolded proDer p 3 wild type and mutants as a function of temperature.</p
AbstractIn a case study on five homologous α-amylases we analyzed the properties of unfolded states ...
The probe concentration in LUVs is 3.6 in. Black lines (■,□) PC LUVs, red lines (●,○) SM/Chol and gr...
The probe concentration in LUVs is 3.6%. (A,B), cPyD9 /iso. (C/D,), cPyO3 /iso. (E), I1/I3 (“polarit...
<p>Far-UV CD (A) and intrinsic Trp fluorescence (B) spectra of the designated proteins (bound with o...
<p>The changes are reflected by (<b>A</b>) synchronous fluorescence for tryptophan emission, (<b>B</...
a<p>(M<sup>−1</sup>s<sup>−1</sup> (×10<sup>5</sup>).</p>b<p>Melting temperature (T<sub>m</sub> in °C...
Time-resolved fluorescence spectroscopy was used to show that multiple tyrosine residues of a protei...
<p>Dark circles represent the experimental data for Wt. Gray and white symbols correspond to Lys107-...
In a case study on five homologous alpha-amylases we analyzed the properties of unfolded states as o...
<p>The protein reconstituted in detergent micelles show one principal transitions in comparison with...
The probe concentration in LUVs is 3.6%. (A), 379 nm cPyD9. (B), 373 nm cPyO3. (C), 388 nm, I3 “cons...
<p>Fluorescence scan diagrams based on <i>Sypro Orange</i> (Thermo Fisher Scientific) binding upon t...
<p>The complete scan for the spectra related to (<b>A</b>) and (<b>B</b>) are presented in <a href="...
<p>(A) Temperature as a function of time during FLIPR temperature-activation assay. (B) Representati...
<p>The fractions of unfolded proDer p 3 wild type and mutants as a function of temperature.</p
AbstractIn a case study on five homologous α-amylases we analyzed the properties of unfolded states ...
The probe concentration in LUVs is 3.6 in. Black lines (■,□) PC LUVs, red lines (●,○) SM/Chol and gr...
The probe concentration in LUVs is 3.6%. (A,B), cPyD9 /iso. (C/D,), cPyO3 /iso. (E), I1/I3 (“polarit...
<p>Far-UV CD (A) and intrinsic Trp fluorescence (B) spectra of the designated proteins (bound with o...
<p>The changes are reflected by (<b>A</b>) synchronous fluorescence for tryptophan emission, (<b>B</...
a<p>(M<sup>−1</sup>s<sup>−1</sup> (×10<sup>5</sup>).</p>b<p>Melting temperature (T<sub>m</sub> in °C...