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. This erroneous model is of interest only because it has been used previously for denatured proteins in studies aimed at correlating m values and ΔC^sub P^ to changes in solventaccessible surface area (90)
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. At any of the explored pH, the percentages of β-hairpin (at 1693 cm^sup -1^) turns/loops/(0, π) β-sheet (at 1679 cm^sup -1^) and antiparallel β-sheet (at 1633 cm^sup -1^) remained essentially unaltered
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. In particular differences in the extent of protein aggregation, in structural compactness, or simply in the structural arrangement of tryptophan residues in unfolded states can change the magnitude of the red shift observed during the unfolding transition significantly
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. Having stressed that the data of Fig
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. Since the dealkylated soman moiety bound to the HuBChE monomer subunit contributes only three hydrogen atoms (P-CH^sub 3^) to the enzyme-inhibitor conjugate, while the deglycosylated native enzyme monomer itself accounts for >3500 nonexchangeable hydrogen atoms, the contribution of the inhibitor is negligibly small
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. In general, the wettability of Sn-2
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. 6, whereas Table 1 collects the data for residues with significant exchange broadening (see table legend for more details)
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. Reference spectra of conformational limits
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. This function accounts, in part, for the anti-atherogenic action of HDL and its major protein, apolipoprotein A-1 (apoA-1, 243 aa) (Barter and Rye, 1996)
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. These include activation or inhibition of plasma enzymes that are essential in reverse cholesterol transport (Forte et al
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. The results help to elucidate the role of apolipoprotein size and hydrophobicity for HDL stability, to uncouple apolipoprotein unfolding, dissociation, and lipoprotein fusion, and thereby gain a better insight into molecular determinants for the structural stability and fusion of HDL disks and spheres
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. This exemplifies that the correct criterion for thermodynamic reversibility is the absence of scan rate effects and hysteresis rather than the repeatability of a transition
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. Trial moves that set backbone torsions are pivot moves because these lead to large-scale conformational changes
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.2 ppm (30)-could be detected (Fig
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.RESULTS AND DISCUSSIONCharacterization of soluble prefibrillar aggregates and protofibrilsGeneration of prefibrillar oligomers of TTR from the A-stateProlonged dialysis of TTR (96 h, 4°C) versus 10 m M HCl in dH^sub 2^O in the absence of salt (pH 2
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. Similar multiphase kinetics of the Gdm-induced unfolding was observed in apoA-1:DMPC disks (Reijngoud and Phillips, 1982) and in apoC-1 disks (unpublished data)
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. To further evaluate the contribution of solvent-induced shifts, we examined a model duplex DNA molecule whose structure is not expected to change significantly with Mg^sup 2+^ concentration changes in the 0
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. Journal of Consulting and Clinical Psychology, 66, 474-483
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