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. In addition, the peak corresponding to tryptophan emission displayed a significant red-shift to [lambda]^sub max^ ~ 334-339 nm
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. Phase diagram analysis of IR and fluorescence data The phase diagram analysis, which is a sensitive tool to detect folding intermediates, was carried out as described previously (35)
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. 8 × 10^sup 3^ M^sup -1^ cm^sup -1^ at 370 nm (25)
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. or 350 nm, after excitation at 280 and 295 nm, with a scan rate of 30 K/h
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. Either we could not unambiguously determine the protein-concentration independence of the thermal midpoint from fluorescence measurements (see above, for the values, and Fig
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. The most rapid components had lifetimes Time-resolved fluorescence anisotropy was employed to probe the dynamics of different conformational states of TTR
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. It should be emphasized that this is not due to loss-of-fluorescence due to titration of ThT, which is the case for, e
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. Apart from the faster kinetics, the increased temperature leads to a more complex morphological variability: long straight rods, twisted ribbonlike structures, rod bundles, and ropelike structures become prominent in the corresponding AFM data
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. Between 2 and 5 M GdnHCl, a significant drop in anisotropy was observed, indicating faster rotational mobility of tryptophan residues upon unfolding of GR
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. As a result, for each sequence, we generated an ensemble consisting of 10^sup 4^ uncorrelated conformations
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