Skip to main content
. Author manuscript; available in PMC: 2007 Aug 28.
Published in final edited form as: J Mol Biol. 2007 Mar 6;368(5):1332–1344. doi: 10.1016/j.jmb.2007.02.078

Figure 1.

Figure 1

Abundance of disulfide-bonded proteins in P. aerophilum, as detected by fluorescent labeling. Whole cell lysate was reacted with iodoacetamide (+) to block free (thiol) cysteines. Following blocking, any disulfide bonds present were cleaved by reduction with TCEP and fluorescently labeled with CPM. When iodoacetamide is omitted (−) all cysteines are labeled. A comparison of corresponding lanes shows that a large fraction of P. aerophilum proteins contain disulfide bonds. E. coli cells serve as a control.