Dr. Wieland Steinchen

Team Leader


Dr. Wieland "Willy" Steinchen




DFG core facility for Interactions, Dynamics and biomolecular Assembly Structure

Proteins exhibit three-dimensional (3D) structures that specify their function. The function of proteins is based on their concise dynamic properties that allow for conformational changes required for their interaction with other proteins and ligands, such as metals, small chemical compounds, peptides, RNA and DNA. Detailed analysis of protein structure and dynamics is crucial for the molecular understanding of biological processes. Protein structure determination has made major progress mainly through X-ray crystallography and nuclear magnetic resonance spectroscopy (NMR).

However, analysis of the dynamic behavior of proteins and their macromolecular assemblies is not straightforward and easy-on methods still lag behind. Although NMR can provide great insights, it is often hampered by the size of a protein or its assembly, and/or by the sample amount and stability during the rather long measurements.

In recent years, Hydrogen-Deuterium eXchange mass spectrometry (HDX) has offered an attractive new route for the analysis of the dynamic behavior and the structural features of proteins and macromolecular assemblies in solution. HDX can be performed with low sample quantities. Moreover, measurements are usually performed in the time scale of seconds to minutes. HDX relies on the principle that the amide protons of all amino acids (except for proline) within the peptide bonds of proteins undergo exchange with deuterium in deuterated or ‘heavy’ water on a time scale that can be measured by mass spectrometry. The hydrogen-to-deuterium exchange rates depend on temperature, pH and the physico-chemical environment in which the respective amide proton is located (i.e.; solvent accessibility and hydrogen bonding).


Recent and selected publications of Dr. Wieland Steinchen


Corrales-Guerrero L, He B, Refes Y, Panis G, Bange G, Viollier PH, Steinchen W*, Thanbichler M* (2020). Molecular architecture of the DNA-binding sites of the P-loop ATPases MipZ and ParA from Caulobacter crescentus. 

Nucleic Acids Research, doi: 10.1093/nar/gkaa192. *Joint corresponding authors

Kunz S, Tribensky A, Steinchen W, Oviedo-Bocanegra L, Bedrunka P, Graumann PL (2020). Cyclic di-GMP Signaling in Bacillus subtilis is governed by direct interactions of Diguanylate Cyclases and Cognate Receptors.

mBIO, 11(2):e03122-19

Skotnicka D, Steinchen W, Szadkowski D, Cadby IT, Lovering AL, Bange G, Sogaard-Andersen L (2020). CdbA is a DNA-binding protein and c-di-GMP receptor important for nucleoid organization and segregation in Myxococcus xanthus.

Nature Communications 11(1):1791

Osorio-Valeriano M, Altegoer F, Steinchen W, Urban S, Liu Y, Bange G, Thanbichler M (2020). ParB-type DNA segregation proteins are CTP-dependent molecular switches.

Cell, 179(7):1512-1524

Han X, Altegoer F, Steinchen W, Binnebesel L, Schuhmacher J, Glatter T, Giammarinaro PI, Djamei A, Rensing SA, Reissmann S, Kahmann R, Bange G (2019). A kiwellin disarms the metabolic activity of a secreted fungal virulence factor.

Nature, 565(7741):650-563

Eckel M, Steinchen W, Batschauer A (2018). ATP boosts lit state formation and activity of Arabidopsis cryptochrome 2.

Plant Journal, 96 (2):389-403

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