Editing Structural biology (section)

== Techniques ==
[[Biomolecule]]s are too small to see in detail even with the most advanced light [[microscope]]s. 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]]
* [[X-ray crystallography#Biological macromolecular crystallography|Macromolecular crystallography]]
* [[Neutron diffraction]]
* [[Proteolysis]]
* [[Nuclear magnetic resonance spectroscopy of proteins]] (NMR)
* [[Electron paramagnetic resonance]] (EPR)
* [[Cryo-electron microscopy|Cryogenic electron microscopy]]  (cryoEM)
* [[Electron crystallography]] and [[microcrystal electron diffraction]]
* [[Multiangle light scattering]]
* [[Biological small-angle scattering|Small angle scattering]]
* [[Ultrafast laser spectroscopy]]
* [[Anisotropic terahertz microspectroscopy]]
* [[Two-dimensional infrared spectroscopy]]
* Dual-polarization interferometry and [[circular dichroism]]
Most often researchers use them to study the "[[native state]]s" of macromolecules. But variations on these methods are also used to watch nascent or [[Denaturation (biochemistry)|denatured]] molecules assume or reassume their native states. See [[protein folding]].

A third approach that structural biologists take to understanding structure is [[bioinformatics]] to look for patterns among the diverse [[DNA sequence|sequence]]s that give rise to particular shapes. Researchers often can deduce aspects of the structure of [[integral membrane protein]]s based on the [[membrane topology]] predicted by [[hydrophobicity analysis]]. See [[protein structure prediction]].