A number of factors have come together in the last couple of decades to
define the emerging interdisciplinary field of structural molecular
biology. First, there has been the considerable growth in our ability to
obtain atomic-resolution structural data for biological molecules in
general, and proteins in particular. This is a result of advances in
technique, both in x-ray crystallography, driven by the development of
electronic detectors and of synchrotron radiation x-ray sources, and by
the development ofNMR techniques which allow for inference of a
three-dimensional structure of a protein in solution. Second, there has
been the enormous development of techniques in DNA engineering which
makes it possible to isolate and clone specific molecules of interest in
sufficient quantities to enable structural measurements. In addition,
the ability to mutate a given amino acid sequence at will has led to a
new branch of biochemistry in which quantitative measurements can be
made assessing the influence of a given amino acid on the function of a
biological molecule. A third factor, resulting from the exponential
increase in computing power available to researchers, has been the
emergence of a growing body of people who can take the structural data
and use it to build atomic-scale models of biomolecules in order to try
and simulate their motions in an aqueous environment, thus helping to
provide answers to one of the most basic questions of molecular biology:
the relation of structure to function.