Per Jemth research group

Per Jemth research group

The ultimate goal of our research is to better understand fundamental structure-function and structure-reactivity relationships in proteins. Our research focuses on the molecular details and evolution of protein-protein interactions, protein folding and function.

Structure-function relationships of proteins

Proteins govern all of life's chemical reactions and they generally do so by first folding into precise three dimensional (3D) structures dictated by their amino acid sequences. But, we have now learned that a a large fraction of our proteome is not folded, instead proteins or certain regions of proteins are disordered. Such intrinsically disordered protein regions (IDRs) lack, in part or completely, a well-defined 3D structure. There is now a tremendous interest in understanding structure, function and dynamics of IDRs. However, despite intense efforts there is still a marked paucity of experimental data regarding many aspects of how disorder influences the function of proteins and how functional disorder has evolved.

We use different model systems, such as binding domains from the transcriptional co-activators CBP/p300, the transactivation domain of p53 and MDM2, and other proteins and binding motifs from animals, bacteria and viruses. An exciting line of research that we pursue is resurrection of ancient proteins, in an effort to understand how intrinsically disordered regions have evolved. In another project we want to understand the structure and function of de novo proteins. These are proteins that only exist in one or a few closely related species, suggesting that they have a recent origin. They are predicted to be disordered. But there is also the exciting possibility that they can fold and if so, which 3D structures do they adopt, new or ancient ones?

We address these questions using a combination of biophysics, protein engineering and phylogenetic methods.

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