Abstract
In order to understand the protein function in detail, it is important to have information on tertiary structure of the protein. Protein tertiary structure has generally been studied using X-ray crystallography and NMR. However, these techniques require a large scale sample preparation. On the other hand, mass spectrometry requires a smaller sample amount and is much faster than X-ray crystallography or NMR. These are great advantages of MS in the structural characterization of a protein. In the present commentary, it will be described how to study the tertiary structure of proteins using hydrogen-deuterium exchange in conjunction with mass spectrometry.
