Professor Dr Angela M. Gronenborn
- Section Biochemistry and Biophysics
- Location Pittsburgh, United States
- Election year 2014
Research
Research Priorities: NMR-spectroscopy, structure analysis, proteins, HIV infection, macromolecular complexes
Angela M. Gronenborn is a chemist and pioneer in the field of multidimensional solution NMR spectroscopy (Nuclear Magnetic Resonance). She researches the structure and cellular interactions of proteins. Some of the first NMR protein structures that were registered in the Protein Data Bank (PDB) came from her laboratory. One focus of her work are the proteins involved in HIV infections.
NMR spectroscopy is one of the main analysis methods in chemistry and is extremely versatile. It allows molecule structures to be depicted in three-dimensional form and the interactions between molecules to be explained. Angela M. Gronenborn developed NMR methods for the structural analysis of proteins and macromolecular complexes. Using these methods she investigates the structure and interactions of viral and cellular proteins as well as their role in HIV-1 infections, one of the two known HI viruses. Her laboratory was able to identify the structures of some HIV and HIV-associated proteins, including the barrier-to-autointegration factor (BAF), the negative regulatory factor (NEF), and proteases. Angela M. Gronenborn wants to use the specific combination of data from solution and solid-state NMR, x-ray crystallography and cryo-electron microscopy to deliver further explanations about the virus’ structure. In doing so, she aims to obtain new insights for the development of medication.
In other work, she researches the structural foundations of carbohydrate recognition by lectins. In addition to NMR and other types of spectroscopy, Angela M. Gronenborn and her team also carry out in-vivo studies. They research on living cells to investigate, in particular, the molecular structures and interactions linked to diseases.
Angela M. Gronenborn is a chemist and pioneer in the field of multidimensional solution NMR spectroscopy (Nuclear Magnetic Resonance). She researches the structure and cellular interactions of proteins. Some of the first NMR protein structures that were registered in the Protein Data Bank (PDB) came from her laboratory. One focus of her work are the proteins involved in HIV infections.
NMR spectroscopy is one of the main analysis methods in chemistry and is extremely versatile. It allows molecule structures to be depicted in three-dimensional form and the interactions between molecules to be explained. Angela M. Gronenborn developed NMR methods for the structural analysis of proteins and macromolecular complexes. Using these methods she investigates the structure and interactions of viral and cellular proteins as well as their role in HIV-1 infections, one of the two known HI viruses. Her laboratory was able to identify the structures of some HIV and HIV-associated proteins, including the barrier-to-autointegration factor (BAF), the negative regulatory factor (NEF), and proteases. Angela M. Gronenborn wants to use the specific combination of data from solution and solid-state NMR, x-ray crystallography and cryo-electron microscopy to deliver further explanations about the virus’ structure. In doing so, she aims to obtain new insights for the development of medication.
In other work, she researches the structural foundations of carbohydrate recognition by lectins. In addition to NMR and other types of spectroscopy, Angela M. Gronenborn and her team also carry out in-vivo studies. They research on living cells to investigate, in particular, the molecular structures and interactions linked to diseases.
Career
- since 2006 Professor, Department of Bioengineering, University of Pittsburgh, Swanson School of Engineering, Pittsburgh, USA
- since 2006 Director, Pittsburgh Center for HIV Protein Interactions (PCHPI), Pittsburgh, USA
- since 2005 UPMC Rosalind Franklin Professor and Head, Department of Structural Biology, School of Medicine, University of Pittsburgh, Pittsburgh, USA
- 2005 Professor, Department of Pharmacology, School of Medicine, University of Pittsburgh, Pittsburgh, USA
- 2004 Visiting Professor, Department of Pharmacology and Director, Structural Biology Program, School of Medicine, University of Pittsburgh, Pittsburgh, USA
- since 1996 Senior Biomedical Research Service (SBRS), National Institutes of Health, USA
- 1991-2005 Head, Structural Biology Section, Laboratory of Chemical Physics, National Institutes of Health, Bethesda, USA
- 1988-2005 Senior Researcher, Laboratory of Chemical Physics, National Institutes of Health (NIH), Bethesda, USA
- 1987 Habilitation in Physical Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany
- 1984-1988 Head, Biological NMR Group, Max Planck Institute of Biochemistry, Martinsried, Germany
- 1979-1984 Researcher, Divisions of Molecular Pharmacology and Physical Biochemistry, National Institute for Medical Research, Mill Hill, London, UK
- 1978 Postdoctoral Fellow, Division of Molecular Pharmacology, National Institute for Medical Research, Mill Hill, London, UK
- 1978 Ph.D. in Organic Chemistry, University of Cologne, Cologne, Germany
- 1975 Diploma, University of Cologne, Cologne, Germany
- 1969-1975 Degree in Chemistry, University of Cologne, Cologne, Germany
Functions
- Member, Advisory Board, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
- Editor, FEBS Journal
Projects
- 2019-2023 Project “Structural characterization of interacting and aggregating cataract-associated crystallins”, National Science Foundation (NSF), USA
- 2017-2021 Principal Investigator, Project “Development of Fluorine Nuclear Magnetic Resonance (NMR) Spectroscopy as a Versatile Probe of Structure and Chemical Environment in Proteins”, NSF, USA
- 2011-2014 Project “Conformation and Dynamics of Cataract Mutants of human gammaD crystallin”, NSF, USA
- 2007-2022 Principal Investigator, Project “Allosteric regulation of SIRT1 by a PACS-2 and DBC1 regulatory hub”, NSF, USA
Honours and Memberships
- 2021 Biophysical Society’s 2021 Founders Award, Biophysical Society, Rockville, USA
- 2020 E. Bright Wilson Award, Spectroskopy, American Chemical Society, USA
- 2019 Richard R. Ernst Prize, Magnetic Resonance, Euromar Conference, Niederlande
- 2019 Mildred Cohn Award, Biological Chemistry, American Society for Biochemistry and Molecular Biology, USA
- seit 2018 Mitglied, American Academy of Arts and Science, USA
- 2015-2018 Einstein Visiting Fellow, Einstein Stiftung, Berlin
- seit 2014 Mitglied, Nationale Akademie der Wissenschaften Leopoldina
- 2014 Life Sciences Award, Carnegie Science Foundation, Washington D.C., USA
- seit 2010 Mitglied, Norwegian Academy of Science and Letters, Norwegen
- seit 2008 Mitglied, International Society of Magnetic Resonance
- seit 2007 Mitglied, National Academy of Science, USA
- 2006 Award for Excellence in Magnetic Resonance, Eastern Analytical Symposium and Exposition, Spring Lake, USA
- seit 2002 Mitglied, American Association for the Advancement of Science (AAAS), USA
- 1992 Director's Award, NIH, Bethesda, USA
- seit 1990 Mitglied, Royal Society of Chemistry, London, UK
- 1989 Scientific Achievement Award, Washington Academy of Sciences, Washington D.C., USA