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EI^sup sc^ was a well-folded turner that could be heat-denatured in a single sigmoidal transition, and thus it followed the second mechanism proposed
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Characlerization of the Exchcrichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy
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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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Thermal behavior of human plasma high density lipoprotein
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The oblique mouth was open by the end of the yolksac larval stage
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After initial fixation the tissue samples were stored in a 0
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055 -2,617 30Average annual effect-15,517
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