Nuclear Magnetic Resonance (NMR) is an important technique for studying proteins at atomic level. In this technique, an organic substance, in this case a protein, is brought into a magnetic field and irradiated with radio waves. Atom nuclei then emit a signal. Ubbink: ‘Since every signal has a slightly different frequency, which can be observed separately, it is as if the protein is covered in ‘antennae’. Each antenna provides information about its own environment around the protein.’ Proteins are complex structures which consist of elastic, dynamic components. The instrument measures these movements over a certain period of time and the researchers then convert these data into images.

By adding an unpaired electron, for instance in the form of a metal atom, to a protein, a strong interaction occurs between the electron and the other atomic nuclei, as a result of which signals can be measured even better. This effect can be used to study how proteins bind with each other, thereby enabling all kinds of processes in the living cell. Ubbink studies the dynamics of protein complexes and has already shown that they attract one other, rotate around one other and briefly connect with one another before releasing one another. Why do proteins do this and what is the equilibrium between dynamics and structure during this short interaction? This also allows for a more accurate study of the mobility of loose proteins and their interactions with smaller molecules, such as drugs.