The Awesome Power of Fluorine NMR
9 May 2019
- University Campus Bohunice (pavilion A11/ seminar room 132)
Prof. Angela Gronenborn
University of Pittsburgh, USA
"My work aims to uncover the structural basis of cellular interactions.
In my research, I ask questions about the molecular and atomic details that govern specificity in the intricate interplay between cellular components that result in the amazing functional diversity observed in living organisms: How do single amino acid changes in proteins cause major conformational changes that result in different protein architectures? Are there general rules that govern protein-ligand recognition? Why are sugars frequently recognized through multi-valent and multisite interactions? What are the fundamental causes for proteins to aggregate as seen in protein deposition diseases? How do specific signaling complexes form malignancies? How does the HIV virus usurp the cellular machinery for its own purposes?
These and related questions are what motivate the broad research program in my lab.
New people and fresh ideas are the lifeblood of all research groups. I encourage you to contact me directly if you have an excellent academic background in chemistry or physics and find yourself interested in the research that we are doing."
See more information at the webpage of Prof. Gronenborn´s group.
About the lecture
19F solution 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 absence in naturally occurring biomolecules, and small size. 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.