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. Author manuscript; available in PMC: 2014 Jul 8.
Published in final edited form as: Amino Acids. 2012 Oct;43(4):1471–1483. doi: 10.1007/s00726-012-1220-3

Figure 5.

Figure 5

Proteolytic stability of Crp4, proCrp4 and various salt-bridge mutated analogues. AU-PAGE analysis of untreated peptides (−) and peptides treated with trypsin. Arrows indicate the bands corresponding to Crp4 and proCrp4. Strikingly native proCrp4 is processed into a native-like form of Crp4, which is stable to further degradation. In contrast all mutant peptides, whether subjected to trypsin as precursors or mature peptides, are fully degraded by trypsin.