Protein-Ligand Interactions, First Edition

✍ Scribed by Raimund Mannhold, Hugo Kubinyi, Gerd Folkers(eds.)

• Year: 2012
• Tongue: English
• Leaves: 347
• Category: Library

✦ Synopsis

Innovative and forward-looking, this volume focuses on recent achievements in this rapidly progressing field and looks at future potential for development.
The first part provides a basic understanding of the factors governing protein-ligand interaction, followed by a comparison of the four key experimental methods (calorimetry, surface plasmon resonance, NMR and X-ray crystallography) used in generating interaction data. The second half of the book is devoted to in-silico methods of modeling and predicting molecular recognition and binding. 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.

✦ Table of Contents

Content:
Chapter 1 Statistical Thermodynamics of Binding and Molecular Recognition Models (pages 1–22): Kim A. Sharp
Chapter 2 Some Practical Rules for the Thermodynamic Optimization of Drug Candidates (pages 23–31): Ernesto Freire
Chapter 3 Enthalpy–Entropy Compensation as Deduced from Measurements of Temperature Dependence (pages 33–43): Athel Cornish?Bowden
Chapter 4 Interaction Kinetic Data Generated by Surface Plasmon Resonance Biosensors and the Use of Kinetic Rate Constants in Lead Generation and Optimization (pages 45–70): U. Helena Danielson
Chapter 5 NMR Methods for the Determination of Protein–Ligand Interactions (pages 71–98): Bernd W. Koenig, Sven Schunke, Matthias Stoldt and Dieter Willbold
Chapter 6 Polarizable Force Fields for Scoring Protein–Ligand Interactions (pages 99–120): Jiajing Zhang, Yue Shi and Pengyu Ren
Chapter 7 Quantum Mechanics in Structure?Based Ligand Design (pages 121–143): Par Soderhjelm, Samuel Genheden and Ulf Ryde
Chapter 8 Hydrophobic Association and Volume?Confined Water Molecules (pages 145–170): Riccardo Baron, Piotr Setny and J. Andrew McCammon
Chapter 9 Implicit Solvent Models and Electrostatics in Molecular Recognition (pages 171–189): Tyler Luchko and David A. Case
Chapter 10 Ligand and Receptor Conformational Energies (pages 191–205): Themis Lazaridis
Chapter 11 Free Energy Calculations in Drug Lead Optimization (pages 207–236): Thomas Steinbrecher
Chapter 12 Scoring Functions for Protein–Ligand Interactions (pages 237–263): Christoph Sotriffer
Chapter 13 Druggability Prediction (pages 265–282): Daniel Alvarez?Garcia, Jesus Seco, Peter Schmidtke and Xavier Barril
Chapter 14 Embracing Protein Plasticity in Ligand Docking (pages 283–294): Manuel Rueda and Ruben Abagyan
Chapter 15 Prospects of Modulating Protein–Protein Interactions (pages 295–329): Shijun Zhong, Taiji Oashi, Wenbo Yu, Paul Shapiro and Alexander D. MacKerell