Research Article
Biochemical and Biophysical Characterization of the Enolase from Helicobacter pylori
Figure 3
Secondary and tertiary structure of enolases. (a) Far-UV circular dichroism spectra; black cross: Streptococcal surface enolase; red line: P. falciparum enolase (dimer); red dashed line: P. falciparum enolase (monomer);pink line with asterisks: S. pyogenes enolase (TME buffer); pink asterisks: S. pyogenes enolase (Glycine buffer); green circles: S. cerevisiae enolase; blue closed squares: apo-HpEno (Tris-HCl); blue open squares: holo-HpEno (Tris-HCl); blue closed triangles: apo-HpEno (potassium phosphate); blue open triangles: holo-HpEno (potassium phosphate). (b) Fluorescence emission spectra for the excitation wavelength of 280 nm; Green closed circles: S. cerevisiae enolase (Tris-acetate); green open circles: S. cerevisiae enolase (Tris-HCl); blue closed squares: apo-HpEno(Tris-HCl); blue stars: apo-HpEno (Tris-acetate). (c) Fluorescence emission spectra for the excitation wavelength of 295 nm; red line: P. falciparum enolase; green open circle: S. cerevisiae enolase (Tris-HCl); blue closed squares: apo-HpEno(Tris-HCl); blue stars: apo-HpEno (Tris-acetate).
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