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. Author manuscript; available in PMC: 2011 Mar 1.
Published in final edited form as: J Am Soc Mass Spectrom. 2009 Oct 29;21(3):323–337. doi: 10.1016/j.jasms.2009.10.013

Figure 4.

Figure 4

Location of the [88-102] segment (highlighted in red) within the crystal structure of IFN (1AU1, panel A) with respect to Cys-17 (highlighted in orange). Alkylation of Cys-17 inevitably leads to steric clashes within the native structure, which can be removed by unfolding of the helix D containing the [88-102] segment (panel B). Side chains of hydrophobic residues within helix D are sequestered in the protein interior (highlighted in green, panel C), but become exposed to solvent upon unfolding of this structural element (panel D).