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. Equilibrium NMR studies of unfolded and partially folded proteins
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. Bis-ANS shows very strong fluorescence in response to all conformational states of TTR, with the strongest signal emanating from the rapidly formed monomeric A-state upon NaCl addition
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. A decrease in conformational entropy after appending a second trajectory that samples a much smaller conformational space than the first one, and is contained in the conformational space of the first trajectory (Fig
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. The inability of two- and three-way junction ribozymes to fully populate a docked conformation reveals the importance of correct helical junction geometry as well as loop elements for effective ribozyme folding
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. Synthesis of soybean agglutinin in bacterial and mammalian cells
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. In all fluorescence experiments the samples were prepared from ANS and protein stocks to a final constant protein concentration of 2 µM in 2 mM Hepes buffer, pH 7
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. Here, the average (τ^sup o^^sub m^)^sub app^ values for the α-helices are given in parentheses and the error on Φ was based on a uniform error in (τ^sup o^^sub m^) of 1
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. The value of v estimated from measurements of the reduced viscosity of dilute solutions of BLG as a function of concentration or from the known dimensions of the dimer is in the range 3
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. The Trp fluorescence of acid unfolded TTR peaks at 352 nm (data not shown) compared to 340 nm in the native protein, indicating unfolding
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. However, repeating this study for solubilized proteins that were freshly dialyzed to remove detergent gave an apparent K^sub d^ only 10-fold weaker than predicted, suggesting that we may be not be viewing a simple protein-protein association (K^sub d^ ~ 70 nM; Fig
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. Data fitting suggests that, in contrast to the double-exponential kinetics in the first jump (τ^sub fast^ = 190 s, τ^sub slow^ = 1630 s), the data in the second jump are well approximated by a single exponent with a relaxation time τ = 190 s, which is similar to τ^sub fast^
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