Cooperations

Department of Biophysics

Research

The Biophysics Department conducts interdisciplinary research at the interface of biomolecular function, physical chemistry and radiochemistry. The activities contribute to the Helmholtz Research Programmes Nuclear Safety and Cancer Research in the Helmholtz-Association. We are member of the Cluster of Excellence "Physics of Life" (PoL) in Dresden.

We are particularly interested in:

structural and dynamic aspects of biomembranes
conformational transitions in membrane proteins
interactions between (radio)metals and biomolecules
effects of metals and radionuclides on the metabolism of microorganisms (Televised MDR report)

Education

The Biophysics department participates in the Dresden International Graduate School for Biomedicine and Bioengineering (DIGS-BB) supported by the Excellence Initiative of the German federal and state governments.

Practicals on Molecular Spectroscopy and Calorimetry are offered. The following lectures are held at the technische Universität Dresden and are elgible for the Master Specialization "Soft Condensed Matter and Biological Physics":

Biological Thermodynamics (English, summer semester)
Biophysical Methods (German, winter semester)

Seminar lectures for the International BIOTEC-Master Programme,

Vibrational Spectroscopy (English)
Absorption and Fluorescence Spectroscopy (English)

Experimental Methods

Fourier transform infrared spectroscopy
Circular dichroism
Static and time-resolved fluorescence spectroscopy
Calorimetry
Mass-Spectroscopy

Spectroscopic data are evaluated in combination with Density Functional Theory to understand photochemoical and photophysical properties of organic complexes of actinides.

Latest publication

Interactions between O-Phospho-L-Serine and Trivalent Metal Ions: Studies in Solution and Solid State

Kunigkeit, J.; Drobot, B.; Goldbach, D.; Paasch, S.; Scholz, G.; Stumpf, T.; Brunner, E.; Kretzschmar, J.

Abstract

Contamination of natural habitats including the food chains by chemotoxic and/or radiotoxic f-elements is a substantial threat for human life. Dairy products are an integral part of the daily diet of various human cultures and contain high amounts of proteins with phosphorylated amino acid residues, especially serine. These proteins are responsible for the ability to bind Ca2+ but they can also bind poisonous f-elements. The present paper aims to characterize the metal-binding properties at the molecular level by studying the interactions of O-phospho-L-serine with selected ions in solution as well as in solid precipitates by the combined application of liquid-state and solid-state nuclear magnetic resonance (NMR) spectroscopy, complemented by time-resolved laser-induced fluorescence spectroscopy (TRLFS). In solution, trivalent ions of lanthanum, europium, and lutetium, as well as of the lighter, NMR-active surrogate yttrium, are primarily coordinated upon bidentate phosphate complexation. In the obtained solids the ligand’s carboxylate group is involved in coordination. Depending on solution conditions, three complex species are forming, one of which prevailing as soluble 1:1 complex species and two of which forming solid phases of 3:2 and 1:1 SerP:metal ratio.

Keywords: Lanthanide; Phosphorylated amino acid; NMR; TRLFS; Complex; Structure elucidation; Stability constant; Radioecology; Milk protein

European Journal of Inorganic Chemistry (2026), e202500480
DOI: 10.1002/ejic.202500480

Permalink: https://www.hzdr.de/publications/Publ-41799

More publications

Team

Name	Bld./Office	+49 351 260	Email
Head
Prof. Dr. Karim Fahmy	801/P301	2952 3601	k.fahmyhzdr.de
Employees
Name	Bld./Office	+49 351 260	Email
Dr. Björn Drobot	801/P302	2978	b.drobothzdr.de
Prof. Dr. Satoru Tsushima	801/P302	2978	s.tsushimahzdr.de
Other employees
Name	Bld./Office	+49 351 260	Email
Dr. Charlotte Kielar	801/P303	3247 3892	c.kielarhzdr.de

Physical Chemistry of Biomolecular Condensates

Name	Bld./Office	+49 351 260	Email
Head
Dr. Ellen Adams	801/P301	2911	e.adamshzdr.de
Employees
Name	Bld./Office	+49 351 260	Email
Artur Czajkowski	801/P303	3375	a.czajkowskihzdr.de
Likhitha Chakra Priya Pulibandla	801/P303	3375	l.pulibandlahzdr.de
Manthan Raj	801/P303	3375	m.rajhzdr.de