Short description Innovative and forward-looking, this volume focuses on recent achievements and looks at potential for future development. Both novices and experts will find this an inspiring and often-consulted guide to the complexity of protein-ligand interaction modeling and analysis.
From the contents PART I: BINDING THERMODYNAMICS Statistical Thermodynamics of Binding and Molecular Recognition Models Some Practical Rules for the Thermodynamic Optimization of Drug Candidates Enthalphy-Entropy Compensation as Deduced from Measurements of Temperature Dependence PART II: LEARNING FROM BIOPHYSICAL EXPERIMENTS Interaction Kinetic Data Generated by Surface Plasmon Resonance Biosensors and the Use of Kinetic Rate Constants in Lead Generation and Optimisation NMR Methods for the Determination of Protein-Ligand Interactions PART III: MODELING PROTEIN-LIGAND INTERACTIONS Polarizable Force Fields for Scoring Protein-Ligand Interactions Quantum Mechanics in Structure-Based Ligand Design Hydrophobic Association and Volume-Confined Water Molecules Implicit Solvent Models and Electrostatics in Molecular Recognition Ligand and Receptor Conformational Energies Free Energy Calculations in Drug Lead Optimization Scoring Functions for Protein-Ligand Interactions PART IV: CHALLENGES IN MOLECULAR RECOGNITION Druggability Prediction Embracing Protein Plasticity in Ligand Docking Prospects of Modulating Protein-Protein Interactions
