Research under high pressure

Why 3,000 bars are needed to take a comprehensive look at a protein

08-May-2024 - Konstanz researchers Frederic Berner and Michael Kovermann present a new high-pressure spectroscopy method to unravel the properties of proteins' native structures. A pressure of 3,000 bar is applied to the cold shock protein B of Bacillus subtilis in a small tube in the NMR spectroscopy ...

Demystifying the 'Parkinson Protein'

Research team succeeds in directly observing the membrane binding of α-synuclein in living cells

11-Mar-2021 - The protein α-synuclein is one of the most abundant proteins in the human brain. It is often referred to as the "Parkinson protein", as deposition of this protein in brain cells is a hallmark of Parkinson's disease. Despite the high interest of biomedical research in the protein, many questions ...

Real-time observation of enzymatic processes on DNA

Insights into the molecular processes involved in the detection of DNA strand breaks

05-May-2020 - DNA strand breaks can contribute to the development of cancer and the ageing process. Researchers from the Departments of Biology and Chemistry of the University of Konstanz have now been able to observe in real time the molecular processes that take place at DNA strand breaks by means of ...

New technique for in-cell distance determination

21-Mar-2019 - Researchers from the University of Konstanz, Bielefeld University and ETH Zurich demonstrate for the first time that the pulsed EPR technique RIDME (relaxation-induced dipolar modulation enhancement) can be used for in-cell distance determination in biomacromolecules. Applied within the cell, ...

Analyzing the structure of the protein FAT10

Fundamental research for a potential cancer therapy

04-Sep-2018 - FAT10 is a small protein with a huge effect. Its attachment to a target protein is a signal for its degradation. FAT10 is a marking system for degradation that seems to be inefficient. In contrast to its biological competitor, ubiquitin, which is recycled, FAT10 is degraded along with its target ...