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. 2010 Oct 1;107(42):17986–17991. doi: 10.1073/pnas.1004823107

Fig. 1.

Fig. 1.

Mapping changes in functional and structural properties caused by point mutations on the amino acid sequence of PYP. The effect of Ala substitutions on visible absorbance maximum λmax, pCA pKa, pCA fluorescence quantum yield Φfl, pB lifetime τpB, thermodynamic stability Inline graphic, and protein production level are shown as the value of [(value of mutant – value of WT)/value of WT]. The secondary structure of PYP is also shown, with α-helices in red, β-strands in blue, and the π-helix in yellow. Positions at which substitutions cause large increases in values are indicated in red, small increases in yellow, large decreases in dark blue, and small decreases in light blue. The same color scheme is used in Figs. 2 and 3 to facilitate visual inspection of the dataset.