Technische Universität München
Professur für Festkörper-NMR-Spektroskopie (Prof. Reif)
Lichtenbergstr. 4
85748 Garching b. München
Our group is interested in the structural characterization of biomolecules using MAS solid-state and solution-state NMR spectroscopy, with focus on amyloidogenic peptides and proteins, and chaperones. Our research is divided into the areas Structural characterization of aggregation inter-mediates and understanding the mechanisms that lead to protein aggregation at atomic resolution, Structure and dynamics of amyloid fibrils, Interactions of small molecules and molecular chaperones which affect the morphology and the toxicity of amyloid aggregate, Investigation of large protein complexes that are not amenable by solution-state NMR or crystallography, Development of methods in MAS solid-state NMR for quantification of structure and dynamics of biomolecules.
Links:
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…
Langmuir
Abstract: The amyloidogenesis of the pancreatic metabolic hormone human islet amyloid polypeptide (hIAPP) is associated with dysfunction of the pancreatic β-cell function in type II diabetes. Although the…
Chemical Communications
Abstract: Nanodiscs are emerging as valuable tools for studying lipid-protein interactions. In this study, we demonstrate the dual role of nanodiscs in modulating human amylin (hIAPP) fibrillation using NMR and…
Journal of the American Chemical Society
Abstract: Deposition of amyloid plaques in the brains of Alzheimer’s disease (AD) patients is a hallmark of the disease. AD plaques consist primarily of the beta-amyloid (Aβ) peptide but can contain other…
Chemistry - A European Journal
Abstract: Amyloid plaques are a major pathological hallmark involved in Alzheimer's disease and consist of deposits of the amyloid-β peptide (Aβ). The aggregation process of Aβ is highly complex, which leads to…
Biomolecular NMR Assignments
Abstract: Amyloid fibrils from Alzheimer’s amyloid-beta peptides (Aβ) are found to be polymorphic. So far, 14 Aβ40 fibril structures have been determined. The mechanism of why one particular protein sequence…
Communications Biology
Abstract: Aggregation of the human islet amyloid polypeptide (hIAPP) contributes to the development and progression of Type 2 Diabetes (T2D). hIAPP aggregates within a few hours at few micromolar concentration…
Proceedings of the National Academy of Sciences of the United States of America
Abstract: Patients with type 1 diabetes mellitus who are dependent on an external supply of insulin develop insulin-derived amyloidosis at the sites of insulin injection. A major component of these plaques is…
Journal of the American Chemical Society
Abstract: The deposition of islet amyloid polypeptide (hIAPP) fibrils is a hallmark of β-cell death in type II diabetes. In this study, we employ state-of-the-art MAS solid-state spectroscopy to investigate the…
Nachrichten aus der Chemie
| Titel | Termine | Dauer | Art | Vortragende/r (Mitwirkende/r) |
|---|---|---|---|---|
| Biochemisches Grundpraktikum (CH0936) |
|
3 | PR | |
| Forschungspraktikum Biochemie 1 (CH0554) |
|
16 | FO | |
| Forschungspraktikum Biochemie 2 (CH0555) |
|
12 | FO | |
| Forschungspraktikum mit chemischem Schwerpunkt (CH0510) |
|
8 | FO | |
| Physikalische Biochemie, Vortragsseminar (CH0410b) |
|
2 | SE | |
| Seminar für wissenschaftliche Mitarbeiter |
|
4 | SE |
| Titel | Termine | Dauer | Art | Vortragende/r (Mitwirkende/r) |
|---|---|---|---|---|
| Biologische Festkörper-NMR (CH5174) |
|
2 | VO | |
| Chemie II (B.Sc. Engineering Science) |
|
3 | VI | |
| Forschungspraktikum Biochemie 1 (CH0554) |
|
16 | FO | |
| Forschungspraktikum Biochemie 2 (CH0555) |
|
12 | FO | |
| Forschungspraktikum mit chemischem Schwerpunkt (CH0510) |
|
8 | FO | |
| Methods of Catalysis (CH3242a) |
|
2 | VO | |
| Methods of Catalysis, Seminar (CH3242b) |
|
1 | SE | |
| Seminar für wissenschaftliche Mitarbeiter |
|
4 | SE |