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. Author manuscript; available in PMC: 2016 Jan 31.
Published in final edited form as: Arch Biochem Biophys. 2014 Dec 19;567:66–74. doi: 10.1016/j.abb.2014.12.014

Fig. 1.

Fig. 1

Structures and mass spectrometry characterization of modified human Shh proteins. (A) Schematic diagram of Shh proteins with selected modifications of the N-terminal cysteine of Shh. The N-terminal residue in processed human ShhN is cysteine 24 and the C-terminal residue is glycine 197. Unmodified ShhN (ShhN), 5-(N-ethyl-malemidyl) modified ShhN (NEM-ShhN), 4-maleimidobenzophenone modified ShhN (Bzm-ShhN) and fluorescein-maleimide modified ShhN (Flu-ShhN). (B) Whole mass spectra of modified human Shh proteins. ESI-MS spectra of modified Shh proteins with expected change in mass for each modifying group noted.