Skip to main content
Fig. 4 | BMC Bioinformatics

Fig. 4

From: A computational method for designing diverse linear epitopes including citrullinated peptides with desired binding affinities to intravenous immunoglobulin

Fig. 4

Diversity of the designed, predicted high- and low-binding affinity peptides. The sequence diversity among the Pythia-design peptides is significantly higher than the approach of [2]. The y-axis gives a measure of diversity of a set of designed peptides (see text) under a particular Hamming-distance threshold defining similar peptides (x-axis). Almost all the Pythia-designed peptides differ in at least 9 of their 15 possible positions

Back to article page