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Mechanisms of Protein Folding
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Reversibility of the thermal transition was examined by reheating the samples after cooling from the first scan
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It can be concluded, then, that EI^sup sc^ at low pH unfolded via a moltenglobule-like species, as it has been described in other large multimeric proteins (49)
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Blood 2004; 103:3362-3364(31) Bose J, Gruber AD, Helming L, et al
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The immersion depth and the immersion speed were 3 mm and 21 mm/sec, respectively
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Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations
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Rheological modeling of microgel suspensions involving solid-liquid transition
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DCVJ has not to our knowledge been used before on an amyloid system but has been employed on microtubule polymerization (Haidekker et al
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5 A, and see below)
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We find that Gα(GDP) significantly decreased the volume change for the CPM-PLCβ-Gβγ association (Table 1)
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This would only occur when the averaged atom-positional fluctuations, i
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. None of these models can provide an accurate description of conformational ensembles accessible to highly denatured proteins since they explicitly disregard the effects of correlated fluctuations imposed by two-body EV interactions
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. Ice-induced ANS binding to other proteins To examine whether the ice-induced perturbation observed for azurin is common to proteins in general, ANS binding experiments were extended to a set of seven other proteins including monomeric BSA, α-amylase and β-gal, dimeric LADH and tetrameric ALD, YADH, and LDH
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.To contribute to the ongoing discussion and to investigate the relationship among molecular dynamics, activity, inhibitor-binding, and unfolding, we carried out incoherent elastic neutron scattering experiments on two members of the cholinesterase (ChE) family: Tetrameric human butyrylcholinesterase (HuBChE), both native and covalently inhibited by the organophosphate nerve agent, soman (18), and dimeric native Drosophila melanogaster acetylcholinesterase (DmAChE)
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. However, almost all of these reports described DNA-monocation interaction without any consideration of the change in the higher-order structure of DNA, which is essential for understanding the role of monocations in DNA compaction in living cells
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