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Thermodynamic and folding properties versus structure among the members of a protein family Early studies suggested that folding and equilibrium pathways of homologous proteins were similar, and that the folding of a certain structure was thus conserved through evolution (58,59)
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. OBi lead-free solder on Cu and Ni substrates was assessed by the wetting balance tests and compared with that of the Sn-Pb solder
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. Therefore, the following studies were conducted assuming that properties of the membrane surface are largely unchanged in the 1-2000 bar range
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. Extended and docked conformations of the hairpin ribozyme were also resolved and quantified in previous ensemble trFRET experiments (N
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- Thus, it seems reasonable to expect that the monomers of yeast GR may also be catalytically inactive and that dimerization may be critical for enzyme activity
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. Due to its important physiological roles in intracellular amino acid metabolism, ACYI deficiency caused by genetic mutation has recently been related to inborn metabolism diseases (12,13)
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. Our results show that dimeric EI^sup sc^ acquired a folded conformation at physiological pH: however, 8-anilino-1-naphthalene-sulfonic acid (ANS)-binding experiments, FTIR, and CD measurements suggested that the protein populated a molten-globule-like species at low pH
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. FTIR spectra in the presence of the effectors were acquired and compared with those obtained in their absence to find out whether there were secondary structural changes upon binding
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.In a first experiment, we compared MSDs of native HuBChE and soman-inhibited HuBChE over a large temperature range (20 to ~349 K), passing the denaturation temperature of native HuBChE
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. Interestingly, the residues with (f = 0
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. The treatment by gender interaction effect was statistically significant (b=2
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