Some of our research projects

Sophia Eiden

For my project I am engaged in the investigation of different types of G-quadruplex DNA or RNA binding proteins which could be identified in a proteomic approach. For this I will perform overexpression and purification of candidate proteins and analyze their interaction with various oligonucleotide structures – not only with G-quadruplex, but also with triplex, double stranded and single stranded nucleic acids.

The project is carried out in cooperation with the Institut Curie in Paris.

Larissa Käver

My research is all about quantification of epigenetic markers along genomic DNA. My focus lies on simultaneous detection of 5mC and 5hmC using two-step DNA modification reactions. First, reactive groups are transferred sequence-specifically using methyltransferases and β-glycosyltransferases. In a second step, bioorthogonal click-chemistry is used to establish fluorescent barcodes on the DNA by fluroescence microscopy. With these barcodes it is possible to obtain quantitative information on the epigenetic state of the DNA substrate.

Felix Gularek

I´m not in the lab anymore as I´m currently writing my thesis. My research is all about DNA barcoding. I use DNA methyltransferases to specifically transfer reporter groups to DNA. The modified DNA molecules are analyzed using fluorescence microscopy and nanopores/nanochannels. Another aspect of my work includes the development of computational methods to quantify the efficiency of a certain DNA barcoding method.

Miriam Rauser

I´m not in the lab anymore and I will have my PhD defence soon. My project is about developing a novel bioconjugation method for covalent protein-plasmid DNA conjugates. To achieve this I combine the methyltransferase transfer of activated groups (mTAG) method with SNAP-tag technology. In the mTAG method the side chain of a S-Adenosyl-L-methionine (AdoMet) analouge is sequence-specifically tansferred to plasmid DNA by DNA methyltransferase. The side chain of the AdoMet analouge includes a O6-benzylguanine (BG) residue. In the SNAP-tag technology the SNAP-tag protein reacts specifically with this BG residue and the conjugate is formed. The SNAP-tag protein is a variant of the human repair enzyme O6-alkyguanin alkytransferase and can be fused to different protein of interest.

Leonie Schütz

My project is about engineering activity DNA methyltransferases with various cofactor analogues for DNA labeling. In cooperation with the group of Giulia Rossetti at the Forschungszentrum Jülich, I am performing computational simulations to dock cofactor-methyltransferase interactions. Results from these in silico experiments are then used to optimize catalytic activities by organic synthesis of new cofactor analogues or site-directed mutagenesis of proteins.

Kerstin Glensk

Much of my work involves protein expression and purification and doing restriction modifications assays.

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Weinhold group, design by: Sabrina Otto, Miriam Rauser, last modified: 17.04.2020 (Leonie Schütz)

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