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Life

What keeps a cell alive? How does an enzyme recognize its substrate, how does a plant protect itself from a pathogen, and why do proteins fold in exactly one single functional way? These fundamental questions drive the researchers in the Department of Chemistry and Biochemistry. Using the tools of modern chemistry, they investigate how biological function arises from structure and intermolecular interaction: through high-resolution structural analysis of proteins and nucleic acids, the targeted synthesis of chemically modified biomolecules and precise intervention in cellular signaling pathways. In this way, research in the department combines a fundamental understanding of biological processes with concrete perspectives for medicine, agriculture and biotechnology.

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Proteins

Proteins are the molecular machines of life: they catalyze biochemical reactions, mediate intercellular signal transmission and form structural scaffolds in tissues and cells. The department's research groups determine protein structures at atomic resolution and analyze how conformational flexibility and post-translational modifications regulate molecular function. Research objects include protein kinases, inhibitory neuroreceptors, extracellular matrix components and proteins involved in the development of neurodegenerative diseases.

This topic brings together

Daniel Friedrich

The Friedrich Lab uses NMR to uncover structure–activity relationships in biomolecular interactions and define molecular principles of biological function. It focuses on dynamic transitions at atomic resolution, enabling the rational design of functional biomolecules.

Günter Schwarz

Protein Structure–Function group investigates protein structure–function relationships ranging from basic metabolism to molecular neuroscience, with a focus on the biosynthesis of the molybdenum cofactor, molybdenum cofactor deficiency, and the structural biology of inhibitory neurotransmitter receptors.

Jan Riemer

The research group investigates redox control of cellular processes and the integration of mitochondria into cellular signaling networks, with a focus on redox homeostasis, mitochondrial biogenesis, proteostasis, and the metabolic regulation of proteome plasticity.

Karsten Niefind

The research group uses X‑ray crystallography to determine the three‑dimensional structures of biologically relevant proteins and enzymes, including eukaryotic protein kinases, plant immune signaling proteins, and enzymes involved in bacterial pollutant degradation and biotechnological applications.

Elmar Behrmann

The research group investigates the structure and dynamics of proteins in functional states. Using cryo‑EM, flexible systems and light‑driven mechanisms are elucidated in near‑native environments to better understand molecular modes of action.

A cluster of crystalline structures radiating from a central point. The crystals feature sharp edges and prismatic shapes, glowing in intense colors such as magenta, yellow, and green against a teal background.

Ulrich Baumann

Structural biology research on the extracellular matrix and proteolytic systems. The research group combines biochemistry, biophysics, and modern methods such as cryo‑EM and X‑ray crystallography to elucidate protein structures and interactions.

Structure

The structural principle of molecular biology states: function follows from structure. In order to elucidate this relationship, the researchers in the department use a wide range of methods, including cryo-electron microscopy, X-ray crystallography, solid-state and solution NMR and mass spectrometry. The three-dimensional structural information obtained in this way forms the molecular basis for the rational design of new active substances and the mechanistic understanding of biological processes.

This topic brings together

Erik Strub

The group is interested in fundamental chemistry of the artificial element Technetium. Further, we collaborate with the institutes of geology and nuclear physics in the field of accelerator mass spectrometry. We are performing radiometric analyses, and apply X-ray Fluorescence for archeometry.

A cluster of crystalline structures radiating from a central point. The crystals feature sharp edges and prismatic shapes, glowing in intense colors such as magenta, yellow, and green against a teal background.

Ulrich Baumann

Structural biology research on the extracellular matrix and proteolytic systems. The research group combines biochemistry, biophysics, and modern methods such as cryo‑EM and X‑ray crystallography to elucidate protein structures and interactions.

Elmar Behrmann

The research group investigates the structure and dynamics of proteins in functional states. Using cryo‑EM, flexible systems and light‑driven mechanisms are elucidated in near‑native environments to better understand molecular modes of action.

Karsten Niefind

The research group uses X‑ray crystallography to determine the three‑dimensional structures of biologically relevant proteins and enzymes, including eukaryotic protein kinases, plant immune signaling proteins, and enzymes involved in bacterial pollutant degradation and biotechnological applications.

Daniel Friedrich

The Friedrich Lab uses NMR to uncover structure–activity relationships in biomolecular interactions and define molecular principles of biological function. It focuses on dynamic transitions at atomic resolution, enabling the rational design of functional biomolecules.

Mathias Schäfer

Mathias Schäfer investigates ionization and fragmentation mechanisms as well as the structural analysis of natural products using tandem mass spectrometry, infrared multiphoton dissociation, photoaction spectroscopy, and ion mobility spectrometry, complemented by quantum-chemical calculations.

Simone Wiegand

The research group investigates transport processes in aqueous systems, particularly thermodiffusion and thermophoresis, and employs optical scattering methods to study the influence of hydration shells and hydrogen bonding on biological and biocompatible compounds.

Enzymes

Enzymes accelerate biochemical reactions under physiological conditions with impressive substrate specificity and catalytic efficiency. The department investigates enzymes both as research objects and as biotechnological tools: for example, for the enzymatic incorporation of artificial nucleotides into nucleic acids, for enantioselective synthesis reactions or to elucidate the molecular causes of metabolic diseases such as molybdenum cofactor deficiency.

This topic brings together

Bernd Goldfuß

Our group investigates the molecular basis of reactivity and selectivity in chemical transformations. Experimental and computational methods support the design of novel catalysts and reagents. Current research focuses on enantioselective hydrogen-bonding and carbocationic catalysts.

Karsten Niefind

The research group uses X‑ray crystallography to determine the three‑dimensional structures of biologically relevant proteins and enzymes, including eukaryotic protein kinases, plant immune signaling proteins, and enzymes involved in bacterial pollutant degradation and biotechnological applications.

Günter Schwarz

Protein Structure–Function group investigates protein structure–function relationships ranging from basic metabolism to molecular neuroscience, with a focus on the biosynthesis of the molybdenum cofactor, molybdenum cofactor deficiency, and the structural biology of inhibitory neurotransmitter receptors.

Redox

Oxidation and reduction processes are fundamental for almost all energy-transferring and regulatory processes in living cells. They link the mitochondrial respiratory chain to cell metabolism, protect against reactive oxygen species and modulate protein functions through reversible oxidation. Researchers in the department are investigating the molecular mechanisms of cellular redox homeostasis and its interrelationship with mitochondrial biogenesis, proteostasis and intracellular signaling networks.

This topic brings together

Günter Schwarz

Protein Structure–Function group investigates protein structure–function relationships ranging from basic metabolism to molecular neuroscience, with a focus on the biosynthesis of the molybdenum cofactor, molybdenum cofactor deficiency, and the structural biology of inhibitory neurotransmitter receptors.

Jan Riemer

The research group investigates redox control of cellular processes and the integration of mitochondria into cellular signaling networks, with a focus on redox homeostasis, mitochondrial biogenesis, proteostasis, and the metabolic regulation of proteome plasticity.

Peptides

Despite their comparatively small size, peptides have a remarkable variety of biological functions as hormones, antimicrobial agents, cell signaling molecules and membrane modulators. Peptides are rationally designed, synthesized and structurally and functionally characterized in the department. A central research focus is on membrane-active and cell-penetrating peptides, which can be used as molecular transporters for the targeted intracellular application of therapeutic agents.

This topic brings together

Daniel Friedrich

The Friedrich Lab uses NMR to uncover structure–activity relationships in biomolecular interactions and define molecular principles of biological function. It focuses on dynamic transitions at atomic resolution, enabling the rational design of functional biomolecules.

Ralf Giernoth

The research group develops switchable molecules and solvents for biomedical applications, investigates ionic liquids and their interactions, and synthesizes novel chiral anions as strong Brønsted acids for asymmetric applications.

Ines Neundorf

The research group develops and investigates membrane‑active and cell‑penetrating peptides. The focus is on synthesis, modification, and functional analysis to selectively modulate cellular processes and for applications in drug delivery and therapy.

Nucleotides

Nucleotides and nucleic acids fulfill diverse cellular functions far beyond their classical role as information carriers: as regulatory RNA molecules, as cofactors of enzymatic reactions and as signaling molecules in immune responses. The department's working groups synthesize chemically modified nucleotide building blocks and develop artificial base pair systems in order to functionally expand the natural genetic code. Fields of application range from EPR-based RNA structure analysis and therapeutic mRNA optimization to the chemical strengthening of plant pathogen defence.

This topic brings together

Daniel Friedrich

The Friedrich Lab uses NMR to uncover structure–activity relationships in biomolecular interactions and define molecular principles of biological function. It focuses on dynamic transitions at atomic resolution, enabling the rational design of functional biomolecules.

Stephanie Kath-Schorr

Kath-Schorr group develops chemically modified nucleic acids with artificial base pairs and novel backbone analogues. The aim is precise labeling and targeted functionalization of RNA for structural studies, therapeutic applications, and the enhancement of plant immune responses.