Research in the Protein Biology Group
Click on the names to learn more about the research in the individual laboratories.
Lars ElgaardIn our work, we study this process of oxidative protein folding and degradation in the endoplasmatic reticulum. Specifically, we investigate a number of enzymes involved in this process, and how the interplay of ER redox enzymes and glutathione modulates the overall endoplasmatic reticulum conditions and how misfolded proteins from the endoplasmatic reticulum are degraded.
Rasmus Hartmann-PetersenIn nature cells are regularly challenged by environmental and physiological stress conditions, which may lead to conformational changes of cell proteins to a non-native form. Also during protein synthesis many requirements must be met for a protein to fold and achieve a functional state, so even in the absence of stressful cellular conditions, misfolded proteins may accumulate and pose a serious threat to the cell. To cope with the presence of misfolded proteins, cells have developed molecular chaperones and the ubiquitin-proteasome system that deftly refold or degrade the misfolded proteins, respectively. We study these mechanisms at the molecular and cellular level primarily using mammalian cells.
Kresten Lindorff-LarsenThe primary tools used in our research are computational methods that we use to study the structure and dynamics of proteins. A particular focus is methods that combine experimental data from NMR spectroscopy with molecular simulations. In one set of studies we combine experiments and simulations to provide a detailed structural interpretation of the experimental data. In another methods to predict what mutations are likely to occur and give rise to drug resistance and what possible mutations giving rise to drug resistance would actually render the enzyme inactive.
Karen SkriverTranscription factors control specific genes throung molecular interactions and are themselves regulated by e.g. ubiquitin-dependent degradation. We study the function of specific transcription factors as regulators and regulates. This involves characterization of DNA-binding mechanisms and intrinsic protein disorder in transcriptional activation networks. In addition, we study the molecular specificity and interactome of components of the ubiquitin-dependent protein degradation system.
Martin WillemoësOur work includes elucidating the mechanism of catalysis and regulation for enzymes involved in complex polysaccharide degradation (amylase, mutanase and alpha-mannosidase), for proteases (HIV protease), antibiotic resistance conferring enzymes like beta-lactamase and small molecule converting enzymes mainly from nucleotide metabolism.
Jakob Rahr WintherMy scientific work is focused on basic aspects of protein chemistry and using molecular biology and molecular genetics to understand structure-function relationships in proteins. The main areas of experience include disulfide bond formation and thiol-disulfide redox reactions, in particular in a chemical/biophysical setting with a strong focus on in vitro characterization.
Atlas of Science
A recent publication from the Linderstrøm-Lang Centre hosted at the Section for Biomolecular Sciences has been selected for publication in Atlas of Science. The paper describes how short intrinsically disordered protein regions, socalled SLIMs, can mediate protein-protein interactions in plant stress response regulation.