ZMB Member Peter Bayer, Research

Protein Structure Determination

The institute of "Structural and Medicinal Biochemistry" focuses on the elucidation of protein-protein and protein-ligand interactions using biochemical and biophysical strategies. The research group resorts to a systematic determination of structures of predominantly human proteins and their macromolecular complexes involved in the process of various posttranslational modification pathways. The major issues to address are those of tyrosine sulphation and prolin directed cis/trans isomerisation. The main tool used for structure determination of biomolecules is NMR-spectroscopy. Steps have been taken to build up a crystallisation facility for subsequent X-ray analysis.

Biochemical Characterisation of Human Parvulins

The human genome encodes two peptidyl prolyl cis/trans isomerases of the Parvulin type. The first member, Pin1, binds to and isomerises phosphorylated Ser/Thr-Pro motifs and thus influences activity, localisation and quality control of phospho-proteins. The second member, Parvulin 14 seems to be implicated in nuclear functions such as chromatin remodelling or transcription. We have determined the solution structures of both proteins and investigate their cellular function by fluorescence microscopy, fractionation studies and molecular biology methods.

Posttranslational Sulphation of Proteins

Sulphation of proteins is a posttranslational modification that has an important role in protein-protein recognition, especially of proteins involved in processes such as immune response, blood clotting or in the viral infection of T-helper lymphocytes (HIV). So far, a hundred sulphated proteins are identified in humans which all seem to be modified by two enzymes, the tyrosyl-protein sulfotransferases (TPSTs). The isoforms TPST1 and 2 are trans-Golgi membrane enzymes able to catalyse the transfer of a sulphate group from the active sulphate carrier 3'-phospho adenosine-5'-phosphosulfate (PAPS) onto a tyrosine residue of a target protein. We are interested in elucidating the structures and functions of the human enzymes TPST and PAPS-Synthetase.

Functional Synthetic Peptides and Miniproteins

In cooperation with the Bioinformatics group of Prof. Daniel Hoffmann we have started to design, produce and investigate (poly-)peptides with predicted biological functions. These biologicals, for instance, aim to work as miniproteins to specially recognise binding epitopes on protein receptors or to fulfill functions as molecular probes in fluorescence spectroscopy or magnetic resonance imaging. BMBF-Project: Structure based design of MRI Probe Molecules for the highly sensitive detection of metastases.

Universität Duisburg-Essen

ZMB
Zentrum für Medizinische Biotechnologie

ZMB Member Peter Bayer, Research

Prof. Dr. Peter Bayer

Research

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