How Fast Are Functional Motions of Protein Machines? A Single-Molecule Perspective
Event details
| Date | 13.05.2019 |
| Hour | 12:15 |
| Speaker | Prof. Gilad Haran, Weizmann Institute of Science, Rehovot (IL) |
| Location | |
| Category | Conferences - Seminars |
WEEKLY BIOENGINEERING COLLOQUIA SERIES
(sandwiches served)
Abstract:
Protein machines carry out multiple tasks in the cell, but their modes of operation are still quite obscure. Single-molecule fluorescence spectroscopy is a powerful tool for exposing function-related motions of such nanomachines. We recently developed novel methodology that allows us to track protein dynamics even on the microsecond time scale. In the lecture, I will show how this analysis helped us understanding the dynamics of two different machines. Surprisingly, internal motions are found to be faster than chemical steps by 2-3 orders of magnitude, which we will try to rationalize in the lecture.
Bio:
Gilad Haran is a Professor in the Department of Chemical and Biological Physics at the Weizmann Institute of Science. He did his Ph.D. in Biophysics at the Weizmann Institute and his post-doc in Chemical Physics in the U. of Pennsylvania. He holds the Hilda Pomeraniec Memorial Professorial Chair. He served as the Dean of the Faculty of Chemistry at Weizmann from 2012 to 2018. His research revolves around studies of single molecules and particles. He is interested in particular in studies of protein folding and dynamics using single-molecule FRET spectroscopy. His lab developed original methods for performing and analyzing single-molecule experiments. He is also studying individual plasmonic devices strongly coupled to molecules and quantum dots. Gilad Haran is a recipient of a 2017 European Research Council Advanced Grant. He was awarded the Weizmann Prize of the Tel Aviv Municipality in 2017 and was elected Biophysical Society Fellow in 2019.
Zoom link for attending remotely: https://epfl.zoom.us/j/724143873
(sandwiches served)
Abstract:
Protein machines carry out multiple tasks in the cell, but their modes of operation are still quite obscure. Single-molecule fluorescence spectroscopy is a powerful tool for exposing function-related motions of such nanomachines. We recently developed novel methodology that allows us to track protein dynamics even on the microsecond time scale. In the lecture, I will show how this analysis helped us understanding the dynamics of two different machines. Surprisingly, internal motions are found to be faster than chemical steps by 2-3 orders of magnitude, which we will try to rationalize in the lecture.
Bio:
Gilad Haran is a Professor in the Department of Chemical and Biological Physics at the Weizmann Institute of Science. He did his Ph.D. in Biophysics at the Weizmann Institute and his post-doc in Chemical Physics in the U. of Pennsylvania. He holds the Hilda Pomeraniec Memorial Professorial Chair. He served as the Dean of the Faculty of Chemistry at Weizmann from 2012 to 2018. His research revolves around studies of single molecules and particles. He is interested in particular in studies of protein folding and dynamics using single-molecule FRET spectroscopy. His lab developed original methods for performing and analyzing single-molecule experiments. He is also studying individual plasmonic devices strongly coupled to molecules and quantum dots. Gilad Haran is a recipient of a 2017 European Research Council Advanced Grant. He was awarded the Weizmann Prize of the Tel Aviv Municipality in 2017 and was elected Biophysical Society Fellow in 2019.
Zoom link for attending remotely: https://epfl.zoom.us/j/724143873
Practical information
- Informed public
- Free
Organizer
Contact
- Institute of Bioengineering (IBI), Christina Mattsson