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. A distinct shoulder ([lambda]^sub max^ ~ 305 nm) corresponding to tyrosine emission (18 Tyr residues in each GR subunit) appeared in the spectrum
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. This medium is designated DMEM/ITS+/TGF-[beta]1 hereafter
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. As we discussed previously (13), the behavior in this study is relevant to globular proteins subjected to osmotic stress in biological situations
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. Hammarström, unpublished) compared to binding at pH 7
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. The time course of the protein unfolding, which was triggered by a rapid increase in the Gdm HCl concentration from 0 to 1-6 M, was monitored by CD at 222 nm (Fig
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. The Θ^sub 222^(t) data show a rapid signal loss at any Gdm HCl concentration, indicating fast unfolding within the dead-time of the experiment (30 s), which precludes its quantitative analysis; the amplitude of this rapid phase increases with increasing denaturant concentration (Fig
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