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. A comparison of the δ and S values of proteins in the EV limit to those of folded proteins is shown in Fig
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. From the difference contact maps, we find that upon folding, specific nonnative local contacts have to be broken (weakened) to make native, nonlocal spatial contacts
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. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
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. Is there or isn't there? The case for (and against) residual structure in chemically denatured proteins
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. The cell holder was continuously filled with dry air
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. Encapsulation techniques, either using liposomes (29) or sol-gel glasses (30,31), have recently been used to trap individual proteins in small molecular voids
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. MSDs increase continuously, but display a dynamical transition at ~200 K
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. A model for serine protease catalysis
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. How soft is a protein? A protein dynamics force constant measured by neutron scattering
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. Prefibrillar amyloidogenic oligomers and protofibrils of misfolded TTR were generated in vitro through induction of the molten globule type A-state from acid unfolded TTR through the addition of NaCl
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. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
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. The rate constants were expressed in units of an experimental reference time, the average burst duration, as discussed later
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. This includes data on body fluid concentrations of substances in normal or therapeutic situations, concentrations in fluids and tissues in instances of toxicity, toxic effects, chemical structures, and brief discussion of analytic procedures for the determination of substances in biological specimens
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. 5 A, which coincided with the fact that major conformational changes occurred in this temperature range
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. Although the thermal unfolding of many proteins can successfully be illustrated by a two-state model, step-wise transitions have been observed in several proteins regardless of whether the process was reversible or irreversible (30,38, 39,49-54)
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