John Wiley & Sons, May 21, 2012 - Medical - 359 pages
Innovative and forward-looking, this volume focuses on recent achievements in this rapidly progressing field and looks at future potential for
The first part provides a basic understanding of the factors governing protein-ligand interactions, followed by a comparison of key experimental methods (calorimetry, surface plasmon resonance, NMR) used in generating interaction data. The second half of the book is devoted to insilico methods of modeling and predicting molecular recognition and binding, ranging from first principles-based to approximate ones. Here,
as elsewhere in the book, emphasis is placed on novel approaches and recent improvements to established methods. The final part looks at
unresolved challenges, and the strategies to address them.
With the content relevant for all drug classes and therapeutic fields, this is an inspiring and often-consulted guide to the complexity of
protein-ligand interaction modeling and analysis for both novices and experts.
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Some Practical Rules for the Thermodynamic Optimization
EnthalpyEntropy Compensation as Deduced from Measurements
Learning from Biophysical Experiments
NMR Methods for the Determination of ProteinLigand Interactions
Modeling ProteinLigand Interactions
Quantum Mechanics in StructureBased Ligand Design
Hydrophobic Association and VolumeConfined
Implicit Solvent Models and Electrostatics in Molecular Recognition
Ligand and Receptor Conformational Energies
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