Per Jemth research group

Louise, Weihua, Zeinab, Eva, Frieda, Elin, Shazeeda, Emma, Per

Structure-function relationships of proteins

The ultimate goal of our research is to better understand fundamental structure-function and structure-reactivity relationships in proteins. Our research focuses on the nature and specificity of protein-ligand and protein-protein interactions, and also on protein folding, stability and allostery. We use protein engineering and biophysics to dissect the chemical reactions of proteins.

We use a number of model systems to address the questions. These model systems are small protein domains from modular proteins, involved in for example scaffolding, signalling and transcription. We are particularly interested in intrinsically disordered proteins. Unlike globular proteins, the disordered ones don't fold into well-defined three-dimensional structures and it appears that the disorder is important for their function. Disordered proteins or protein domains are often involved in protein-protein interactions and one famous member of this "class" is p53, which contains both ordered and disordered domains.

The lab is also running a project on a protein from human papillomavirus, namely E6. Certain strains of human papillomavirus cause cancer, for example cervival cancer, and this discovery was awarded the Nobel prize in physiology or medicin in 2008. The E6 protein is a so-called oncogene, and one of the main culprits in the carcinogenesis. If E6 is inhibited the cell will regain control over the cell cycle. We are therefore designing binders toward the E6 protein that may be used to treat HPV-induced cancer.

Please contact us if you are interested in doing a MSc project in the lab. Right now we offer projects about (i) the evolution and/or mechanism of intrinsically disordered proteins and (ii) the design of protein drugs toward HPV E6.

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