Publications by authors named "Adeline Bieker"
Membrane proteins act as a central interface between the extracellular environment and the intracellular response and as such represent one of the most important classes of drug targets. The characterization of the molecular properties of integral membrane proteins, such as topology and interdomain interaction, is key to a fundamental understanding of their function. Atomic force microscopy (AFM) and force spectroscopy have the intrinsic capabilities of investigating these properties in a near-native setting.
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- The study utilized multiple techniques (like ITC, FRET, CD, AFM, DFS, and SPR) to explore how the PhoB protein binds to DNA and how dimerization affects this interaction.
- The research specifically focused on a trimeric complex made of two PhoB proteins and a single DNA oligonucleotide, revealing a positive cooperative binding mechanism that enhances stability.
- Analyzing point mutants and comparing data from different methods helped distinguish binding types and highlighted the importance of using various approaches to fully understand protein-DNA interactions.
Compatible solutes are small, uncharged, zwitter ionic, osmotically active molecules produced and accumulated by microorganisms inside their cell to counteract different kinds of environmental stress. They enhance protein stability without interfering with the metabolic pathways even at molar concentrations. In this paper, we report the stabilizing effects of compatible solutes, ectoine, betaine and taurine on membrane protein bacteriorhodopsin at different concentrations.
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