Technische Universität München
Lehrstuhl für Biotechnologie (Prof. Buchner)
Ernst-Otto-Fischer-Str. 8
85748 Garching b. München
Proteins are involved in almost all biological processes, and their function depends primarily on the correct three-dimensional folding of the polypeptide chain. However, these structures must be dynamic and flexible, to exercise their biological function. As a result, the intrinsic stability of proteins is usually low. As the protein concentration in the cell is very high, this can lead to the interaction of partially folded proteins enhancing their non-specific aggregation. To counteract these limitations, cells have evolved a machinery of molecular chaperones which supports the folding of proteins. We aim for the characterization of spontaneous and chaperone-assisted protein folding and association with a view to define molecular mechanisms and biotechnological applications.
We are engaged in 3 major research areas.
- Analysis of the heat shock protein 90 and 70 (Hsp90, Hsp70) family
- Small heat shock proteins (sHsps)
- Antibodies as bio-therapeutics and antibody-based diseases (AL).
Molecular Cell
Abstract: The Hsp90 molecular chaperone system is regulated by numerous co-chaperones that modulate its function. In Saccharomyces cerevisiae , most of these cofactors can be deleted without affecting…
Nature Communications
Abstract: Binding of the surrogate light chain (SLC) to the heavy chain (HC) of the pre-B cell receptor (preBCR) is an important quality control checkpoint during B cell development as roughly 50% of the…
EMBO Journal
Abstract: Polymeric IgM immunoglobulins have high avidity for antigen and complement, and dominate primary antibody responses. They are produced either as assemblies of six µ2L2 subunits (i.e., hexam-ers), or…
FEBS Letters
Abstract: The diphthamide modification of eukaryotic translation elongation factor (eEF2) is important for accurate protein synthesis. While the enzymes for diphthamide synthesis are known, coordination of eEF2…
Biological Chemistry
BioDrugs
Abstract: Immunoglobulin M (IgM) antibodies are an essential and conserved part of adaptive immunity. IgMs assemble into pentamers and hexamers that bind to antigens with high avidity. Pentamers incorporate a…
Biological Chemistry
Abstract: The molecular chaperone Hsp90 is the central element of a chaperone machinery in the cytosol of eukaryotic cells that is characterized by a large number of structurally and functionally different…
Trends in Biochemical Sciences
Abstract: Small heat shock proteins (sHsps) are an important part of the cellular system maintaining protein homeostasis under physiological and stress conditions. As molecular chaperones, they form complexes…
Nature Communications
Abstract: Hsp90 is a molecular chaperone of central importance for protein homeostasis in the cytosol of eukaryotic cells, with key functional and structural traits conserved from yeast to man. During…
Protein Science
Abstract: The antigen-binding sites in conventional antibodies are formed by hypervariable complementarity-determining regions (CDRs) from both heavy chains (HCs) and light chains (LCs). A deviation from this…
