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Christina Divne

Professor of Structural Biology

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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.

Anders Friberg
Ann Cornell
Antonius van Maris
Arnold Neville Pears
Benoit Baudry
Carina Lagergren
Christer Fuglesang
Christina Divne
Dimos Dimarogonas
Hans Edin
Henrik Boström
Jean-Marc Battini
Magnus Wiktorsson
Martin Monperrus
Michael Malkoch
Monica Bellgran
Nicole Kringos
Panagiotis Papadimitratos
Torbjörn Gräslund
Yusak Octavius Susilo