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. Author manuscript; available in PMC: 2010 May 25.
Published in final edited form as: Chem Biol. 2009 Nov 25;16(11):1169. doi: 10.1016/j.chembiol.2009.10.009

Figure 1.

Figure 1

Neptune spectra and sequence. (A) Absorbance spectra of oxyhemoglobin (red), deoxyhemoglobin (dotted red), mKate (green dashed), mKate S158C (orange), mKate2 (dotted black), Neptune (dashed blue), and mNeptune (light blue). Units are M-1cm-1 versus nm. Hemoglobin spectra are previously published (Stamatas et al., 2006). Inset: Purified mCherry, mKate, S158C, and Neptune proteins at 0.5 mg/mL in visible light. (B) Normalized excitation (left) and emission (right) spectra of mKate (green dashed), mKate S158C (orange), Neptune (dashed blue), and mNeptune (light blue). mKate2 excitation and emission spectra are identical to mKate, as described (Shcherbo et al., 2009). (C) Sequence of mNeptune aligned with its parent, mKate. Changes responsible for the red shift are highlighted in red. The additional monomerization mutation to create mNeptune from Neptune is highlighted in green.