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Figure 4
Alternative linking strategies. The left column indicates the modification. The middle column shows the superposition of each Fab–alternative cyclic peptide complex (colored C atoms) on the Fab–acetylated-amidated disulfide peptide (white C atoms). The right column is the corresponding SPR trace. In all cases, the linking atoms are shifted away from the Val9/Ile10 residues and thus do not pack as well. The affinity of the aminoheptanoic acid linker (AHA) was the closest to the original disulfide meditope.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 72| Part 6| June 2016| Pages 434-442
doi:10.1107/S2053230X16007202
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