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Figure 2 | BMC Biochemistry

Figure 2

From: Differential roles of tryptophan residues in conformational stability of Porphyromonas gingivalis HmuY hemophore

Figure 2

Intrinsic tryptophan fluorescence spectra of apoform and holoform of HmuY alanine-substituted (A) and tyrosine-substituted (B) protein variants. Emission spectra of 4 μM protein samples in 20 mM sodium phosphate buffer, pH 7.4, containing 20 mM NaCl were recorded between 300 and 450 nm at excitation at 295 nm. Overlapping curves marked with arrows correspond to (A) holoHmuY, holoW51A, and holoW161A or (B) holoHmuY, holoW51Y, and holoW161Y. Representative data out of three independent experiments are shown.

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