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. Author manuscript; available in PMC: 2015 Dec 1.
Published in final edited form as: Proteins. 2014 Oct 10;82(12):3373–3384. doi: 10.1002/prot.24692

Figure 6. p53(1–93) fluorescence spectrum and acrylamide induced quenching of tryptophan fluorescence.

Figure 6

Panel A shows the fluorescence spectrum of p53(1–93) measured at 20°C using excitation wavelengths of 280 nm (filled markers) and 295 nm (open markers). Panel B provides Stern-Volmer plots of acrylamide induced quenching of tryptophan at 20°C. Both panels used circles for wild type, squares for ALA−, triangles for PRO−, and diamonds for ALA−PRO−. NATA is shown in panel B using (X). In both panels, fluorescence was measured using 0.5 µM p53(1–93) or 1.5 µM NATA buffered at pH 7 with 10 mM sodium phosphate, 100 mM sodium chloride.