Accounting for side-chain flexibility in protein-ligand docking: 3D Interaction Homology as an approach of quantifying side-chain flexibility of Tyrosine.

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Presentation transcript:

Accounting for side-chain flexibility in protein-ligand docking: 3D Interaction Homology as an approach of quantifying side-chain flexibility of Tyrosine Rotamers

Homology modeling

Protein-Ligand Docking

Conformational selection model

Conformational selection model

Amino Acid Rotamers

HINT Hydropathy: favorable polar (e.g., hydrogen bonding, Lewis acid-base, attractive Coulombic, etc.); unfavorable polar (e.g., Lewis acid-acid and base-base, repulsive Coulombic, etc.); favorable hydrophobic (hydrophobic-hydrophobic, p-stacking, etc.); unfavorable hydrophobic (hydrophobic-polar, desol- vation, etc.).

Ramachandran plots

HINT scoring and basis Map

Average Maps

Average Maps

Conformational Analysis

Results

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