User:Ghuske/Structural biology

History
Draft Outline: Add history section, take methods section and put into its own techniques section.

In 1912 Max Von Laue directed X-Ray's at crystallized copper sulfate generating a diffraction pattern. These experiments led to the development of X-Ray Crystallography, and its usage in exploring biological structures. Pepsin crystals were the first proteins to be crystallized for use in X-Ray diffraction, by Theodore Svedberg. The first tertiary protein structure, that of Myoglobin, was published in 1958 by John Kendrew. During this time, modeling of protein structures was done using balsa wood or wire models. With the invention of modeling software such as CCP4 in the late 1970's, modeling is now done with computer assistance. Recent developments in the field have included the generation of X-Ray free electron lasers, allowing analysis of previously hidden structures and the use of structural biology in assisting synthetic biology
 * Discuss invention of NMR, Electron microscopy,, and their innovators.
 * Discuss modern day innovation and methods briefly
 * Discuss modern day innovation and methods briefly

Techniques
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:


 * Mass spectrometry
 * Macromolecular crystallography
 * Neutron diffraction
 * Proteolysis
 * Nuclear magnetic resonance spectroscopy of proteins (NMR)
 * Electron paramagnetic resonance (EPR)
 * Cryogenic Electron Microscopy (cryoEM)
 * Electron crystallography and Microcrystal electron diffraction
 * Multiangle light scattering
 * Small angle scattering
 * Ultrafast laser spectroscopy
 * Dual-polarization interferometry and circular dichroism

-Copied from Structural Biology, see page history for attribution.