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Christina Divne

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.

Belongs to: About KTH
Last changed: Dec 21, 2017
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