A5085922097- Protein Structure and Dynamics
- Enzyme Structure and Function
- RNA Research and Splicing
- RNA and protein synthesis mechanisms
- Advanced Fluorescence Microscopy Techniques
- Hemoglobin structure and function
- Advanced NMR Techniques and Applications
- Bacterial Genetics and Biotechnology
- Innovative Microfluidic and Catalytic Techniques Innovation
- Microfluidic and Capillary Electrophoresis Applications
- Spectroscopy and Quantum Chemical Studies
- Monoclonal and Polyclonal Antibodies Research
- Electrowetting and Microfluidic Technologies
- Distributed and Parallel Computing Systems
University of Zurich
2016-2023
There has been a long-standing controversy regarding the effect of chemical denaturants on dimensions unfolded and intrinsically disordered proteins: A wide range experimental techniques suggest that polypeptide chains expand with increasing denaturant concentration, but several studies using small-angle X-ray scattering (SAXS) have reported no such increase radius gyration (Rg). This inconsistency challenges our current understanding mechanism denaturants, which are widely employed to...
Chemical denaturants are the most commonly used agents for unfolding proteins and thought to act by better solvating unfolded state. Improved solvation is expected lead an expansion of chains with increasing denaturant concentration, providing a sensitive probe action. However, experiments have so far yielded qualitatively different results concerning effects chemical denaturation. Studies using Förster resonance energy transfer (FRET) other methods found increase in radius gyration but...
Intrinsically disordered proteins (IDPs) abound in cellular regulation. Their interactions are often transitory and highly sensitive to salt concentration posttranslational modifications. However, little is known about the effect of macromolecular crowding on kinetics stability IDPs with their targets. Here, we investigate influence coupled folding binding between two IDPs, using polyethylene glycol as a agent across broad size range. Single-molecule F\"orster resonance energy transfer...
Abstract The association of biomolecules is the elementary event communication in biology. Most mechanistic information how interactions between binding partners form or break is, however, hidden transition paths, very short parts molecular trajectories from encounter two molecules to formation a stable complex. Here we use single-molecule spectroscopy measure path times for intrinsically disordered proteins that folded dimer upon binding. results reveal metastable complex electrostatically...
Intrinsically disordered proteins (IDPs) play key roles in cellular regulation, including signal transduction, transcription, and cell-cycle control. Accordingly, IDPs can commonly interact with numerous different target proteins, their interaction networks are expected to be highly regulated. However, many of the underlying regulatory mechanisms have remained unclear. Here, we examine representative case nuclear coactivator binding domain (NCBD) large multidomain protein CBP, a hub...