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Structural biology
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Structural biology is a branch of molecular biology concerned with the study of the architecture and shape of biological macromolecules—proteins and nucleic acids in particular—and what causes them to have the structures they have. This subject is of great interest to biologists, because macromolecules carry out most of the functions of a cell, and because typically it only is by coiling into a specific three-dimensional shape that they are able to perform their functions. This shape, which is called the "tertiary structure" of a molecule, depends in a complicated way on the molecule's basic composition, or "primary structure."
Biomolecules are too small to see in detail even with the most advanced light microscopes. The methods that structural biologists use to determine their structures generally involve measurements on vast numbers of identical molecules at the same time. These methods include crystallography, NMR, ultra fast laser spectroscopy, electron microscopy, electron cryomicroscopy (cryo-EM), and circular dichroism. Most often researchers use them to study the static "native states" of macromolecules. But variations on these methods are also used to watch nascent or denatured molecules assume or reassume their native states (see e.g. protein folding).
A third approach that structural biologists take to understanding structure is
bioinformatics to look for patterns among the diverse
sequences that give rise to particular shapes. Researchers often can deduce aspects of the structure of
integral membrane proteins based on the
membrane topology predicted by
hydrophobicity analysis. See:
protein structure prediction.
In the past few years it has become possible for highly accurate physical
molecular models to complement the
in silico study of biological structures. Rapid prototyping technologies such as those used by 3D Molecular Design, or the creation of
molecular models in glass by Luminorum Ltd, are notable examples of recent advances in this field.
See also
