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. Upon freezing the sample, the ANS intensity first decreases in the low concentration range, below 80 µM, but then rises sharply above this threshold
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. They generally have k^sup -1^^sub ex^ values below 100 µs confirming the trend
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. from Columbia University and an M
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. Investigation of the properties of these partially folded states using probes such as ANS or bis-ANS (which bind to exposed hydrophobic domains in proteins) was not possible due to the significant overlap between the emission spectra of these probes when bound to proteins and the excitation spectrum of the prosthetic group, FAD (data not shown)
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. Stability of EI^sup sc^ as monitored by DSC and thermal denaturations From the spectroscopic results above, it can be concluded that EI^sup sc^ acquired a folded conformation around physiological pH, and that this structure was basically unaltered (exeept for changes in the ellipticity, Fig
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. It removes the cut, torn and folded metal from the surface that is produced by the previous machining or grinding operation
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. Our experiments are consistent with soman-induced stabilization resulting from an elevation of the free energy of the unfolded state, which arises mainly from a decrease in its entropy due to the covalent modification by soman
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. Therefore, Pb, Ag, or Bi does not contribute to forming intermetallic compounds (IMCs) and only the Cu-Sn IMCs were found for both Sn-Pb and SnAg-Cu-Bi solders with Cu substrates, as shown in Fig
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.1 was examined more extensively, resulting in the nonequilibrium phase diagram shown in Fig
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.20 mg/ml unfolded TTR at pH 2
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.Fluorescence characterization of different protein conformersThe A-state of TTR binds the classic hydrophobic dye ANS (Lai et al
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. The complete reaction can, for simplicity, be divided into four phases, which are schematically depicted in Fig
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., 1997; Sipe and Cohen, 2000; Jackson and Clarke, 2000; Serpell, 2000; Dobson, 2003; Rochet et al
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. semifasciata has a quadrangulate anterior end and a margin almost straight, whereas the margin of the dentary in P
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