Michael Kovermann
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High-resolution NMR spectroscopic approaches to quantify PET microplastics pollution in environmental freshwater samples Open
Reliable identification and precise quantification of microplastics pollution of the environment are essential prerequisites to comprehend the impact of microplastics on Earth's ecosystems. In this study, we propose a workflow to examine p…
Biochemical and Structural Consequences of NEDD8 Acetylation Open
Similar to ubiquitin, the ubiquitin‐like protein NEDD8 is not only conjugated to other proteins but is itself subject to posttranslational modifications including lysine acetylation. Yet, compared to ubiquitin, only little is known about t…
Including the Ensemble of Unstructured Conformations in the Analysis of Protein's Native State by High‐Pressure NMR Spectroscopy Open
The analysis of pressure induced changes in the chemical shift of proteins allows statements on structural fluctuations proteins exhibit at ambient pressure. The inherent issue of separating general pressure effects from structural related…
Targeted Preparation and NMR Spectroscopic Characterization of Lys11‐Linked Ubiquitin Trimers Open
Ubiquitylation refers to the attachment of mono‐ or poly‐ubiquitin molecules to a substrate protein. To shield ubiquitin chains against potential hydrolysis, a facile, click‐chemistry based approach was recently established for the generat…
View article: The Mycobacterium tuberculosis protein tyrosine phosphatase MptpA features a pH dependent activity overlapping the bacterium sensitivity to acidic conditions
The Mycobacterium tuberculosis protein tyrosine phosphatase MptpA features a pH dependent activity overlapping the bacterium sensitivity to acidic conditions Open
The Mycobacterium tuberculosis low-molecular weight protein tyrosine phosphatase (MptpA) is responsible for the inhibition of phagosome-lysosome fusion and is essential for the bacterium pathogenicity. This inhibition implies that M. tuber…
Distinct growth regimes of α-synuclein amyloid elongation Open
Addition of amyloid seeds to aggregation-prone monomers allows for amyloid fiber growth (elongation) omitting slow nucleation. We here combine Thioflavin T fluorescence (probing formation of amyloids) and solution-state NMR spectroscopy (p…
Identification of novel functional mini-receptors by combinatorial screening of split-WW domains Open
A combinatorial approach toward novel functional WW domains based on coiled-coil-mediated reconstitution of split WW domains is presented. As such, an ATP-binding WW domain was found from a 4-by-6 library of N- and C-terminal WW domain fra…
Completing the family of human Eps15 homology domains: Solution structure of the internal Eps15 homology domain of γ‐synergin Open
Eps15 homology (EH) domains are universal interaction domains to establish networks of protein–protein interactions in the cell. These networks mainly coordinate cellular functions including endocytosis, actin remodeling, and other intrace…
Structural and functional consequences of NEDD8 phosphorylation Open
Ubiquitin (Ub) and Ub-like proteins (Ubls) such as NEDD8 are best known for their function as covalent modifiers of other proteins but they are also themselves subject to post-translational modifications including phosphorylation. While fu…
Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate Open
The determination of the binding affinity quantifying the interaction between proteins and nucleic acids is of crucial interest in biological and chemical research. Here, we have made use of site‐specific fluorine labeling of the cold shoc…
All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy Open
The high density of macromolecules affecting proteins due to volume exclusion has been discussed in theory but numerous in vivo experiments cannot be sufficiently understood taking only pure entropic stabilization into account. Here, we sh…
Template-assisted design of monomeric polyQ models to unravel the unique role of glutamine side chains in disease-related aggregation Open
PolyQ model peptides reveal the effect of individual glutamine side chains on fibril formation.
Insights into Protein Stability in Cell Lysate by <sup>19</sup>F NMR Spectroscopy Open
In living organisms, protein folding and function take place in an inhomogeneous, highly crowded environment possessing a concentration of diverse macromolecules of up to 400 g/L. It has been shown that the intracellular environment has a …
Liquid Metastable Precursors of Ibuprofen as Aqueous Nucleation Intermediates Open
The nucleation mechanism of crystals of small organic molecules, postulated based on computer simulations, still lacks experimental evidence. In this study we designed an experimental approach to monitor the early stages of the crystalliza…
Structural and catalytic insights into HoLaMa, a derivative of Klenow DNA polymerase lacking the proofreading domain Open
We report here on the stability and catalytic properties of the HoLaMa DNA polymerase, a Klenow sub-fragment lacking the 3'-5' exonuclease domain. HoLaMa was overexpressed in Escherichia coli, and the enzyme was purified by means of standa…
Crowding-Induced Elongated Conformation of Urea-Unfolded Apoazurin: Investigating the Role of Crowder Shape in Silico Open
Here, we show by solution nuclear magnetic resonance measurements that the urea-unfolded protein apoazurin becomes elongated when the synthetic crowding agent dextran 20 is present, in contrast to the prediction from the macromolecular cro…
Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy Open
As one of the most prevalent post‐translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can b…
Targeted expression and purification of fluorine labelled cold shock protein B by using an auxotrophic strategy Open
High resolution NMR spectroscopy is a seminal method in modern structural biology to obtain insights into proteins' structure, dynamics and function at dilute condition as well as in a cell-like environment or even intracellularly. Usually…
Macromolecular Crowding Tunes Protein Stability by Manipulating Solvent Accessibility Open
In all intracellular processes, protein structure and dynamics are subject to the influence of macromolecular crowding (MC). Here, the impact of MC agents of different types and sizes on the model protein Bacillus subtilis Cold shock prote…
Structural basis for ligand binding to an enzyme by a conformational selection pathway Open
Significance Cellular chemical reactions are slow, and to make them compatible with biological life, enzymes have evolved to accelerate their associated rate constants. Enzymatic catalysis is a complex process where the increase of rate co…
Linkage between Fitness of Yeast Cells and Adenylate Kinase Catalysis Open
Enzymes have evolved with highly specific values of their catalytic parameters kcat and KM. This poses fundamental biological questions about the selection pressures responsible for evolutionary tuning of these parameters. Here we are addr…