Leading NIH Scientist Recruited To Direct New Structural Biology Program At University Of Pittsburgh School Of Medicine
PITTSBURGH, November 17, 2004 An internationally renowned structural biologist has been recruited from the National Institutes of Health (NIH) to direct the new Structural Biology Program at the University of Pittsburgh School of Medicine. Angela M. Gronenborn, Ph.D., who has joined the schools faculty as a professor in the department of pharmacology, will oversee the development and growth of the Structural Biology Program as well as its move next year to 32,000-square-feet of devoted space in the Biomedical Science Tower 3 (BST3), which is now under construction.
Dr. Gronenborn is well recognized by the scientific community for her contributions to the fields of biochemistry and structural biology and is considered a leading expert in nuclear magnetic resonance (NMR) spectroscopy, a method that provides information about the physical and chemical properties of molecules. For the last 13 years she has served as chief of the Structural Biology Section in the Laboratory of Chemical Physics at NIHs National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK).
Dr. Gronenborn is a preeminent scientist who in the last two decades has significantly advanced the field of structural biology and NMR spectroscopy, which has resulted in better understanding of cellular processes at the molecular and atomic levels in relation to human disease. She is truly an important addition to our faculty at a time when there is tremendous potential for further discovery, said Arthur S. Levine, M.D., senior vice chancellor for the Health Sciences and dean, University of Pittsburgh School of Medicine.
Structural biology is a discipline that explores the architecture and organization of proteins, lipids and nucleic acids the building blocks of cells and how they move and interact within the cellular environment. Such information can help pinpoint the specific cause of disease and is essential for the development of more precise and targeted drug therapies. To gain understanding of the shape and configuration of these so-called biomolecules, researchers look at their construction the precise location of atoms in 3-dimensional space using such methods as X-ray crystallography, NMR spectroscopy and electron microscopy. More than a third of the programs space in BST3 will house state-of-the-art instrumentation that supports the use of these techniques.
While at NIH, Dr. Gronenborn and her lab developed 3- and 4-dimensional NMR methods, and more recently, techniques for macromolecule alignment approaches that provide significantly more detailed information about protein structures and are widely used by laboratories worldwide. In 1988, the first protein NMR structures to appear in the Protein Data Bank, an international resource for biomedical research, came from her lab. In addition, she is credited with developing a novel way to label DNA with isotopes, which has made it feasible to use heteronuclear, multidimensional NMR spectroscopic methods to study nucleic acids and their complexes. Previously, such methods could only be applied to the study of protein structures, but now researchers can gain high quality structural information about both protein and DNA molecules and their relation to each other.
Dr. Gronenborn attended the University of Cologne in West Germany, where she received undergraduate and masters degrees in chemistry, and in 1978, a doctorate in organic chemistry, summa cum laude. She undertook post-doctoral training in the Division of Molecular Pharmacology at the National Institute for Medical Research in London from 1978 to 1979, and subsequently became a member of the scientific staff in the divisions of Molecular Pharmacology and Physical Biochemistry from 1979 to 1984. In 1984, she moved to the Max-Planck Institute for Biochemistry in Munich as head of the Biological NMR Group, and in 1988, she joined the NIH as a senior investigator in the Laboratory of Chemical Physics at NIDDK. She was named chief of the laboratorys Structural Biology Section in 1991.
Dr. Gronenborn enjoys prestige as an elected fellow of the Royal Society of Chemistry, the Washington Academy of Sciences and the American Association for the Advancement of Science and as an elected member of the Council of the International Society of Magnetic Resonance, the major international body of scientists pursuing magnetic resonance spectroscopy. She is associate editor of both the Journal of Magnetic Resonance and Magnetic Resonance in Chemistry, serves on editorial boards of five other journals and contributes as a member or advisor to numerous scientific committees and organizations. She has authored or co-authored more than 360 scientific publications and speaks regularly at prestigious national and international meetings.