Data Supplement
- Supplemental Data -
Supplemental Table 1 - Hydrogen bonds with more than 40% of occurrence between 32TRQRY36-NH2 (corresponding to PYY and truncated analogs peptides) and WT-hY2
Supplemental Table 2 - Ki values of PYY-(3-36) analogues for WT-hY2 and its mutants. The Ki value of PYY-(3-36) for the WT-hY2 (0.46 nM), as determined with SPA assay method, was used as a reference to calculate the fold changes of Ki values of other analogues and mutants, indicated in parenthesis
Supplemental Table 3 - Additional mutations generated along this project, all of which revealed to have negligible effects on PYY-(3-36) binding
Supplemental Table 4 - Free energies of binding (in kcal/mol) of PYY for the hY2 mutants, calculated by FEP, and experimental valuesa
Supplemental Figure 1 - Sequence alignment of the NPY and PYY peptides
Supplemental Figure 2 - Sequence and chemical formulae of PYY and analogues
Supplemental Figure 3 - Analysis of the secondary structure in time for PYY peptide and shorter analogues in complex with Y2
Supplemental Figure 4 - Analysis of the secondary structure in time for PYY peptide and shorter analogues in water
Supplemental Figure 5. Scatter plot of the calculated (Y axis) versus experimental (X axis) relative binding free energies (DDG, kcal/mol) for PYY-(3-36) to nine selected hY2 mutants compared to WT-hY2