The 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 transac￾tions 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 mole￾cular 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