Even the first protein structural models were built using X-ray crystallography and NMR spectroscopy sixty and thirty years ago, respectively. There are still many protein sequences and protein complexes with unknown 3-D structure. The tremendous progress in mass spectrometry in last decades opened the space for studying protein folding, protein/ligand interactions and protein dynamics in solution. The potential of ion mobility, chemical cross-linking and hydrogen/deuterium exchange for structural biology will be discussed.
This work has been supported by grants from the Ministry of Education, Youth and Sports of the Czech Republic (LH15010, LD15089), the Czech Science Foundation (16-24309S) and European Regional Development Funds (CZ.1.05/1.1.00/02.0109).