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. 2013 Apr 10;3:1639. doi: 10.1038/srep01639

Table 1. Peptide numbering, sequence, inhibition constants, and binding energy as determined by fluorescence polarization (FP). The variable residues at the p+3 position are highlighted in bold. IC50 values were obtained from competitive binding experiments, converted to Ki according to the Coleska-Wang equation42, and ΔG calculated from the relationship, ΔG = RT ln Ki. Each value represents an average of 4 separate experiments.

# Peptide Sequence Ki (μM) ΔG (kcal·mol−1)
1 pYTPEP 1.3 ± 0.6 −7.95 ± 0.21
2 pYTPAP 18.1 ± 5.7 −6.53 ± 0.22
3 pYTPPP 5.0 ± 2.2 −7.32 ± 0.30