Using only computers, a research team at Uppsala University in Sweden has managed to reveal both the structure and the function of a newly discovered enzyme from the most dangerous malaria parasite, Plasmodium falciparum. All that was needed was the amino acid sequence of the enzyme. The findings may represent a breakthrough for future pharmaceutical research.
The research was carried out within the framework of a project (RAPID) at the Uppsala University Center for Structural Biology, Medical Chemistry, and Computer Chemistry, which was established last year and is directed by Professor Alwyn Jones. The aim is to develop drugs for some of the most severe and widely spread diseases in the world, such as malaria and TB. The results, which recently came out as an “accelerated publication” in the journal Biochemistry, are the work of Professor Johan Åqvist and doctoral student Sinisa Bjelic.
“The enzyme we studied is a new type, with previously unknown catalyst groups. This made it especially interesting as a target molecule for new drugs. Using only computer calculations, we succeeded in revealing both what it looks like and how it functions. It’s the first time anybody ever did that,” says Johan Åqvist.
Anneli Waara | alfa
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The Max Planck Institute for Physics (MPP) is opening up a new research field. A workshop from November 21 - 22, 2016 will mark the start of activities for an innovative axion experiment. Axions are still only purely hypothetical particles. Their detection could solve two fundamental problems in particle physics: What dark matter consists of and why it has not yet been possible to directly observe a CP violation for the strong interaction.
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