The human body contains about a hundred trillion cells. Within each cell are many thousands of different kinds of proteins.
Proteins interact with each other and other molecules, for example DNA. These interactions trigger the vast number of different cell functions. In other words, proteins are the “work horses” of cells enabling the myriad of cellular functions at the molecular level.
The Faculty of Graduate Studies and the Biological Sciences Seminar Series have invited Olaf Jahn, one of the leading protein analysts in the world, to discuss his research on Friday, Aug. 19, 2:15 p.m., in MC H313. The event is open to everyone in the Brock community and all are encouraged to attend this international research presentation.
Jahn is with the Proteomics Group, Max Planck-Institute of Experimental Medicine, Göttingen, Germany.
Jens Coorssen, Dean of the Faculty of Graduate Studies, says the presentation is a rare opportunity for the larger Brock community to connect with a top calibre international researcher from Germany’s renowned Max Planck Society, an organization that funds a network of 83 institutes and research facilities known for excellence in a full range of academic fields.
“Dr. Jahn is one of the key players in large-scale protein analysis, globally,” says Coorssen who held a Fellowship at the Max Planck Institute for Medical Research (Heidelberg). “Analyzing proteins is the only direct route that we have to understand the molecular mechanisms underlying healthy vs disease states.”
Proteomics — the large-scale study of proteins — is a rapidly growing field of modern molecular biology/physiology and the cornerstone of Systems Biology, adds Coorssen.
“Research in this field is focused on understanding normal functions and dysfunctions — that is disease states — at the molecular level, enabling identification of key molecular components and their critical roles,” he explains.
Jahn is a founding member and current speaker of the Göttingen Proteomics Forum. The organization was established in 2004 as a local network of scientists of the Georg-August-University, the University Medical Center Göttingen (UMG), and the Max-Planck Institutes (MPI) of Experimental Medicine and Biophysical Chemistry with the common interest in the analysis of proteins by mass spectrometry.
In addition to his talk, Jahn will be touring Brock’s research facilities and will meet informally with faculty and student researchers.
“This visit has great potential for conversations that can lead to research linkages with Dr. Jahn, his colleagues and the range of Max Planck Institutes,” says Coorssen.
Jahn’s particular specialty is in neuroproteomics that focuses on studying the complex mysteries of neurological diseases. Drug addiction, neurodegeneration, brain injury and nerve growth are some examples of areas in which neuroproteomic research approaches are being applied.
Jahn’s field of interest is in:
- Myelin proteomics
- Synaptic protein networks
- Biomarkers for neurological diseases
- Proteomics automation
- Characterization of biomolecular interactions by photoaffinity labeling and Mass Spectrometry
Biological Sciences Seminar Series presents:
Olaf Jahn, of the Proteomics Group, Max Planck-Institute of Experimental Medicine, Göttingen, Germany, Friday, Aug. 19, 2:15 p.m., in MC H313
Title: “Systematic and structural neuroproteomics: ‘Proteomic phenotyping’ of mutant mice and conformational analysis of synaptic protein complexes.
Abstract: We look at molecular neuroscientific questions from two different proteomic angles. We use systematic approaches such as proteome-wide label-free quantification to understand the biology and pathology of myelin, a plasma membrane specialization of glial cells that facilitates rapid signal propagation along vertebrate axons. The technical advances presented are paving the way for quantitative comparison of myelin proteomes from mutant mice or patient material, and thus for new insights into how axon-glial interactions fail in neurological disorders. Our structural biology approaches, on the other hand, are centered around protein interactions in defined systems and technically live from cross-linking techniques in general and photoaffinity labeling (PAL) in particular. The potential of PAL for gaining structural insights into peptide-protein interactions will be exemplified by our work on Munc13 proteins, which are essential regulators of synaptic vesicle priming and play a key role in adaptive synaptic plasticity phenomena. Our structural data, together with functional evidence, indicate that calmodulin-dependent regulation of synaptic activity is structurally and functionally conserved in all four Munc13 isoforms through non-conserved calmodulin-binding sites.