抄録
Protein dynamics is a basis for understanding the structure-function relationships of proteins, then the magnitude and time scale of fluctuation have been widely investigated by means of various spectroscopic and relaxation methods: B-factor of X-ray crystallography, order parameter of NMR, and compressibility, etc. Among them, hydrogen/deuterium (H/D) exchange kinetics is a novel technique, which gives important information on the proton exchange rate and the number of exchangeable protons. H/D exchange of proteins has been mainly monitored by IR and NMR, but mass spectrometry has been recently utilized in this area. Mass spectrometry has various advantages: the mass change by H/D exchange can be measured with an accuracy of 1 Da using only small amount of sample even if it is a mixture involving some conformers. In this paper, we briefly introduce our method to study the H/D exchange kinetics using a MALDI-TOF-MS coupled with pepsin digestion.
