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Therefore, the K^sub SV^ of 40 M^sup -1^ obtained for iodide quenching of GR in the presence of 7 M GdnHCl suggests that the Trp residues of the protein are significantly, if not completely, exposed to the solvent
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Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain 16 E2 DNA binding protein
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Although a quantitative relation between aggregation and reduction of the unfolding induced red shifts cannot be given, our data indicate that protein aggregation contributes significantly to smaller magnitudes of red shifts as observed during thermal unfolding
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Their main utility is to compare differences in the ANS binding propensity among proteins or brought about by changing experimental conditions such as ice temperature, freezing protocols, or the addition of solutes
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ANS shows a significant burst amplitude (A-state formation) followed by a slow phase in response to oligomeric aggregates
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This same volume change is obtained for a peptide derived from Gβ which also activates PLCβ
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Flexural rigidity was measured with an FRL cantilever bending tester (Testing Machines Inc
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For example, the ability to distinguish between one or two ribozyme conformers in the trFRET analysis is based on the goodness of fit obtained using unimodal or bimodal donor-acceptor distance distribution models
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One quarter of the ad-initiated doctor-patient conversations lead to diagnoses of treatable problems that might have gone undetected, the doctors report
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- The hypocrisies are boundless, and include adoring praise of the deeply oppressive, religiously intolerant Saudi regime side by side with condemnations of democratic Israel
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. Protein concentration was determined by the Lowry method (Lowry et al
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. It has been proposed that the catalytic domain contains a β-sheet sandwiched between α-helices and a second β-sheet located on the surface, whereas the dimerization domain consists of a β-sheet flanked on one side by two α-helices (17)
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. The helix-loop-helix motif formed by the α-helix 9-α-helix 10 shows intermonomer salt bridges: Asp^sup 540^ in the motif with Arg^sup 422^' in α-helix 5 from the other monomer (the prime is used to designate residues in the other monomer)
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. Rather solvent accessible tryptophan residues in the folded state (Fig
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. In this case, however, stabilization of the native state is most probably due to a decrease in free energy of the native state; phosphate, like sulfate, is a salting-out ion that stabilizes folded protein structures and favors aggregation and precipitation
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. Bis-ANS has a shorter lifetime than ANS but also displays two different components with a more even distribution
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. Second, the heat-unfolding curve of the apoA-2:DMPC disks is sigmoidal and is shifted to higher temperatures as compared to that of free protein; thus the unfolding of free apoA-2 is complete at 80°C, well below the apparent melting temperature T^sub m^ = 84°C of the apoA-2:DMPC complexes observed at this scan rate (Fig
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. Insulin fibrils feature characteristics common to all amyloids: x-ray diffraction patterns; affinity to Congo Red and Thioflavin T; birefringence; biological dysfunction and high stability against temperature; pressure; low pH; and proteases
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., 1995), "diffusion-collision" (Karplus and Weaver, 1976, 1994), "nucleation-condensation" (Fersht, 1999), and "topomer search" (Makarov and Plaxco, 2003) models
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. In the context of the three-helix protein, the necessary non-specific interactions are those that keep the first and third helices in contact
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. A constant crystallization temperature is observed in this polymer concentration range
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. Folding of the hairpin ribozyme in its natural conformation achieves close physical proximity of the loops
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