Science Advances

Supplementary Materials

This PDF file includes:

  • Text S1. Theoretical proof of the H-bond pairing principle.
  • Text S2. Relationship between the free energy change for a reversible protein-ligand H-bond competing process and the H-bonding capability of the H-bond–forming atoms.
  • Text S3. The H-bonding capability of the protein atoms with which a ligand atom interacts and the effect of H-bond geometry on the H-bond interaction.
  • Fig. S1. Schematic illustration of the free energy change for the H-bond competing process.
  • Fig. S2. Calculation of H-bonding capability based on water/hexadecane partition coefficients.
  • Fig. S3. Contributions of the H-bonds between CN and the Tyr-OH from scytalone dehydratase to protein-ligand interactions.
  • Fig. S4. Proof for the strong H-bond interactions between the CN group of inhibitor 2 and tyrosine hydroxyls from scytalone dehydratase.
  • Fig. S5. Binding affinities of 1H-imidazole-2-sulfonamide and thiophene-2-sulfonamide.
  • Fig. S6. Quaternary ammonium cation –N(Me)3+-π interactions are more favorable than ammonium ion (–NH3+)-π interactions.
  • Fig. S7. A pathogenic role for the s-s/w-w H-bonding principle in melanin toxicity.
  • Fig. S8. The thermodynamic cycle that demonstrates the contribution of H-bonds to enzymatic catalytic power equates to their contribution to protein-ligand binding.
  • References (46–52)

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