As organisms become increasingly complex, so too must they evolve a more sophisticated molecular alphabet. The recent discovery of proteins that can adopt multiple structural states is one way of addressing this complexity and it has dramatically changed our view of the protein structure-function paradigm.
Almost 40% of the human proteome is predicted to consist of proteins that contain long disordered regions and therefore lack a stable, well-defined three-dimensional structure. These so-called intrinsically disordered proteins (IDPs) have sometimes been referred to as belonging to the dark proteome since they are outside the scope of traditional structural proteomics techniques. IDPs are prevalent in cellular regulation and signaling processes, and are implicated in a vast array of diseases and pathologies.
To study such structurally complex molecules we employ advanced single-molecule spectroscopy techniques, usually in combination with Förster resonance energy transfer (FRET). Single-molecule FRET is a sensitive molecular ruler that allows us to measure molecular distance distributions and dynamics on a broad timescale from picoseconds to hours. A unifying theme of our research is the application of single-molecule techniques to study structurally heterogeneous proteins, especially those found in the nucleus of human cells where they play central roles in chromatin organisation and molecular chaperoning.
We are particularly interested in nucleic acid binding proteins and the complex interplay between proteins and DNA. Our research therefore covers a broad range of molecular processes from signaling to transcription and cellular reprogramming mechanisms.
Our lab is part of the Science Institute and the Biomedical Center, both within the University of Iceland, and we are affiliated with the REPIN Centre at the University of Copenhagen. Our research is funded by grants from the Icelandic Centre for Research (Rannís), University of Iceland, and the Icelandic Cancer Society.
- Heidarsson et al. (2021) Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein, Nat Chem (Accepted).
- Bjarnason et al. (2021) Protein intrinsic disorder on a dynamic nucleosomal landscape, Progress in Molecular Biology and Translational Science (In press).
- Sottini et al. (2020) Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes, Nat Commun 11, 1-14.
- Schuler et al. (2020) Binding without folding- The biomolecular function of disordered polyelectrolyte complexes, Curr Opin Struct Biol 60, 66-76.
- Borgia et al. (2018) Extreme disorder in an ultrahigh-affinity protein complex, Nature 555, 61-66.