Statistical Mechanics, Protein Structure, And Protein Substrate Interactions (nato Science Series B:)
by Sebastian Doniach /
2013 / English / PDF
18.3 MB Download
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.
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.