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. 2012 Mar 12;109(13):4857-4862. doi: 10.1073/pnas.1118157109

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Fig. 2. — Correlating fitness at 30 °C with molecular properties. (A) Fitness measured at 30 °C by competing 27 DHFR mutant strains with a reference WT DHFR strain is plotted against insoluble fraction of DHFR proteins determined in cell lysates by Western blot. Fitness of the WT DHFR strain and its abundance in the insoluble fraction is set to one. (B) Soluble protein abundance (blue circles) determined for single DHFR mutant strains is plotted against apparent midtransition temperature of unfolding () measured in vitro by DSC. Protein abundance predicted at 30 °C by Eq. 1 is depicted in red. Predicted fraction somewhat deviates from a plateau because of the experimental imprecision of ΔG values derived from the urea unfolding under two-state assumption and values inferred from the DSC thermograms (Fig. S4). (C) Fitness measured at 30 °C by competing 27 DHFR mutant strains with a reference WT DHFR strain is plotted against soluble fraction of DHFR proteins determined in cell lysates by Western blot. Fitness of the WT DHFR strain and its abundance in the soluble fraction is set to one.

Inline graphic — Correlating fitness at 30 °C with molecular properties. (A) Fitness measured at 30 °C by competing 27 DHFR mutant strains with a reference WT DHFR strain is plotted against insoluble fraction of DHFR proteins determined in cell lysates by Western blot. Fitness of the WT DHFR strain and its abundance in the insoluble fraction is set to one. (B) Soluble protein abundance (blue circles) determined for single DHFR mutant strains is plotted against apparent midtransition temperature of unfolding () measured in vitro by DSC. Protein abundance predicted at 30 °C by Eq. 1 is depicted in red. Predicted fraction somewhat deviates from a plateau because of the experimental imprecision of ΔG values derived from the urea unfolding under two-state assumption and values inferred from the DSC thermograms (Fig. S4). (C) Fitness measured at 30 °C by competing 27 DHFR mutant strains with a reference WT DHFR strain is plotted against soluble fraction of DHFR proteins determined in cell lysates by Western blot. Fitness of the WT DHFR strain and its abundance in the soluble fraction is set to one.