Professor Angela M. Gronenborn

Professor Angela M. Gronenborn
Department of Structural Biology and Pittsburgh Center for HIV-Protein Interaction
University of Pittsburgh School of Medicine
Host: Professor William Pomerantz

Abstract

The awesome power of fluorine NMR

¹⁹F NMR is a powerful and versatile tool to study protein structure and protein ligand interactions due to the favorable NMR characteristics of the ¹⁹F atom, its small size and absence in naturally occurring biomolecules. ¹⁹F atoms can be introduced readily into proteins and ligands, permitting to use them as ‘beacons’ to study interactions by NMR. Both, ligand and protein resonances can be exploited for this purpose. I will discuss several applications, involving ¹⁹F-modified proteins and ¹⁹F-containing ligands, demonstrating the awesome power of ¹⁹F NMR.

Angela M. Gronenborn

Dr. Angela Gronenborn heads the Department of Structural Biology at the University of Pittsburgh School of Medicine and holds the UPMC Rosalind Franklin Chair. Throughout her career, Dr. Gronenborn was involved in developing NMR methodology for structure determination of biological macromolecules. In the area of HIV research, Dr. Gronenborn directs the Pittsburgh Center for HIV Protein Interactions (PCHPI). In recent years, Dr. Gronenborn has focused on extending the application of NMR to the study of complex systems, in particular developing fluorine NMR approaches. Dr. Gronenborn is an elected Fellow of the Royal Society of Chemistry, U.K., the American Association for the Advancement of Science and the International Society of Magnetic Resonance. She is a member of the Washington and New York Academies of Sciences and was elected to the National Academy of Sciences, the Norwegian Academy of Arts and Letters, the German National Academy of Sciences and the American Academy of Arts & Sciences.