Skip to main content
Figure 2 | PMC Biophysics

Figure 2

From: Inverse tuning of metal binding affinity and protein stability by altering charged coordination residues in designed calcium binding proteins

Figure 2

Conformational analysis by far-UV-CD and Trp fluorescence. (A) The far-UV CD spectra of all 7E15 variants in the presence of 1 mM EGTA or 10 mM Ca2+ in 10 mM Tris, pH 7.4 show a single negative maximum at ~216 nm. CD2 with Ca2+ (open circle), EEDDQ with EGTA (open diamond) or Ca2+ (solid diamond), and EENDN with EGTA (open triangle) or Ca2+ (solid triangle) are shown as examples. (B) The normalized Trp fluorescence spectra for all 7E15 variants almost overlap with a single emission maximum at 327 nm. CD2(open circle), EEDDN with EGTA (open diamond) or Ca2+ (solid diamond), and EEDDE with EGTA (open triangle) or Ca2+ (solid triangle) are shown as examples.

Back to article page