Professor of Structural Biology
Enzymes are proteins which, as biological catalysts, enable all life-sustaining chemical reactions in an organism. These nanomachines are exquisite examples of beauty combined with functional perfection. A typical protein is around six nanometres in diameter, which is only six millionths of a millimetre, and contains around three thousand atoms.
By determining the exact positions of all atoms, we can gain a three-dimensional image of how the enzyme looks, but also understand the enzyme's natural biological function. The structure is determined by exposing the protein crystals to X-rays, which creates a diffraction pattern from which it is possible to determine atom positions and calculate a complete three-dimensional structure.
The atomic structure also provides the knowledge necessary for rational enzyme design, which entails applying a biotechnological process to use structural information to change and adapt the enzyme's catalytic properties for new purposes. This might e.g. be to replace a chemical catalytic reaction in an industrial process and thereby make it more environmentally friendly. The structural information is also the basis for structure-based drug design intended to create more selective and effective drugs with fewer adverse effects.