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. Titration of reactive thiol groupsThis was performed by following the increase in 2-nitro-5-thiobenzoic acid (TNB) absorbance at 412 nm, according to Collier (1973)
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. Massey and Williams (1965) found 3
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. , 1997), suggesting a high degree of intersubunit cooperativity in the reactivation of the enzyme
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. Growing a complex structure such as the vertebrate eye seems to require less energy than growing a fatty plug over a degenerated eye
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. Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins
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. Simulated data agree with theoretical predictions and the agreement is quantified in tenus of residuals between the theoretical distribution and those from simulations
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. Am J Respir Crit Care Med 2005; 172: 465-469(64) Rouhani FN, Meitin CA, Kaler M, et al
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. The observed red shift is caused by the fact that tryptophan residues are replaced from the less-polar interior of the protein to solvent exposed regions upon unfolding
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. laevis oocyte, it is several hundred times that of nuclear DNA (39)
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. If a protein packs well with the membrane interface, then pressure is not expected to destabilize its membrane interactions
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. , 1976; Ritter and Scanu, 1979; Massey et al
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. These results suggest that apoA-1 is a more efficient inhibitor of disk fusion than apoA-2
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. No toner was produced from EVA 40% because phase separation did not occur upon cooling
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. The likelihood of yolked oocytes reaching the developing embryo stage increased with maternal age
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. Our identifying assumption in this and all other regressions is that the pre-RP trends in the outcome variable would have continued into the post-RP period had RP not been implemented
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. The averaged spectrum was used as a reference
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. Although in a system as complex as the PTS, it is likely that more than one form of regulation must exist, the existence of the monomer-dimer equilibrium and the non-sugar specificity of EI make this protein an excellent target to control different cellular functions (such as transport and chemotaxis) (5) and to understand the protein-protein interactions in the PTS
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. However, the herein-observed morphological variation after increasing temperature bears a more profound meaning in light of the ongoing debate as to the identity of the protein's aggregation-prone conformation (completely unfolded, or partly unfolded protein) and our own study, showing that under similar conditions, bovine insulin is substantially more unfolded at 70 than at 60°C (Dzwolak et al, 2003)
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. We note that variations of [gamma] as a function of solvent could potentially produce shifts in peak position in the histograms
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