Dr. Beat Vogeli, University of Colorado
Host: Dr. Venditti
Proteins composed of multiple domains allow for structural heterogeneity and interdomain dynamics that may be vital for function. Intradomain structures and dynamics can influence interdomain conformations and vice versa. However, no established structure determination method is currently available that can probe the coupling of these motions. In this talk, I present a new method based on nuclear and electron magnetic resonance to study, at atomic resolution, the interdomain allosteric pathways in the two-domain cell regulator Pin1 that isomerizes peptidyl-prolines.
Beat Vögeli received B.S. and M.S. degrees in Physics and a Ph.D. degree in Physical Chemistry at ETH Zürich, Switzerland. After a postdoctoral stay at the National Institutes of Health, Bethesda USA, he returned to ETH Zürich to become Oberassistant and then Privatdozent. He is currently an assistant professor at the University of Colorado at Denver in the Department of Biochemistry and Molecular Genetics. He has expertise in NMR spectroscopy of proteins and nucleic acids, and develops methodology for the elucidation of their structures, dynamics and interactions.