Podjarny A., Dejaegere A., Kieffer B. (Eds.) Biophysical Approaches Determining Ligand Binding to Biomolecular Targets: Detection, Measurement and Modelling

The Royal Society of Chemistry, Cambridge, UK, 2011. — 373 p. — ISBN: 1849730091
RSC Biomolecular Sciences, №22The specific recognition of one molecule by another lies at the heart of all biomolecular processes. It is difficult to think of any area of biology where such interactions are not central, providing the super-structures that define cellular systems, selectivity that ensures fidelity in DNA and RNA transactions and underlying the integrity of all metabolic and catabolic reactions. Although the early realisation that such specific interactions are vital came in the late 19th century (Fischer’s lock and key hypothesis) it was not until the 1960s that methods began to be available that could characterize such molecular interactions in detail. Arguably it is only in the past ten years that the methods have gained the sensitivity and applicability to be applied routinely to the study of biological systems.
This book is about the modern methods available to study the binding of ligands to biological molecules. Although the methods have application across the spectrum of biomolecular systems, the techniques have primarily been developed and applied to the study of ligands (usually small molecules) binding to globular proteins in solution. The different chapters review the different
biophysical techniques and their application. Three main themes recur throughout the book: identifying which molecules bind; characterising the structure of the complex; and providing some insights into the thermodynamics and kinetics of binding.
The binding of small ligands to biological molecules is central to most aspects of biological function. The past twenty years has seen the development of an increasing armoury of biophysical methods that not only detect such binding, but also provide varying degrees of information about the kinetics, thermodynamics and structural aspects of the process.Introduction: The Who, Where, Why Questions
Nuclear Magnetic Resonance of Ligand Binding to Proteins
Ligand Binding: The Crystallographic Approach
Surface Plasmon Resonance
Fluorescence Techniques to Characterise Ligand Binding to Proteins
Native Electrospray Ionisation Mass Spectrometry for the Characterisation of Protein/Ligand Systems
Circular Dichroism
Protein Thermal Denaturation Measurements via a Fluorescent Dye
Characterisation of Ligand Binding by Calorimetry
Molecular Modelling of Ligand–Macromolecule Complexes