Chaperoning Single Proteins
Event details
| Date | 04.03.2016 |
| Hour | 12:15 |
| Speaker | Prof. Sander J. Tans, AMOLF, Amsterdam (NL) |
| Location | |
| Category | Conferences - Seminars |
SEMINARS IN BIOLOGICAL PHYSICS
Abstract:
Various chaperones are known to bind exposed protein chains, and hence protect them from aggregation before folding starts, and to rescue them when they are misfolded. Using optical tweezers, we explore how chaperones affect the stability and structure of transient folding intermediates. We show that various chaperones interact directly with folded protein structures, and hence actively help solve their conformational search for the native state. They exploit diverse mechanisms, ranging from stimulating local folding to ATP-driven capture and release of partially folded protein structures. The results indicate that chaperones perform more intricate tasks than previously assumed, and bring a new perspective to the protein-folding problem.
Bio:
Education:
Ph.D. in Physics, Dekker group, Delft University of Technology, 1998
Highest honors, Thesis title: ‘Electron transport in single molecular wires’
M.Sc. in Physics, Mooij group, Delft University of Technology, 1993
M.Sc. in Applied Physics, Université Jussieu, Paris, 1991
Positions:
2001–present
Group leader, FOM-Institute for Atomic and Molecular Physics (AMOLF), Amsterdam, NL
2009–present
Professor, Kavli Institute of NanoScience, Bionanoscience department, Delft University of Technology, NL
1999–2001
Postdoctoral research fellow, Carlos Bustamante group, University of California at Berkeley, USA
1999
Postdoctoral research fellow, Cees Dekker group, Delft University of Technology, NL
1998–1999
I.B.M. Netherlands
Abstract:
Various chaperones are known to bind exposed protein chains, and hence protect them from aggregation before folding starts, and to rescue them when they are misfolded. Using optical tweezers, we explore how chaperones affect the stability and structure of transient folding intermediates. We show that various chaperones interact directly with folded protein structures, and hence actively help solve their conformational search for the native state. They exploit diverse mechanisms, ranging from stimulating local folding to ATP-driven capture and release of partially folded protein structures. The results indicate that chaperones perform more intricate tasks than previously assumed, and bring a new perspective to the protein-folding problem.
Bio:
Education:
Ph.D. in Physics, Dekker group, Delft University of Technology, 1998
Highest honors, Thesis title: ‘Electron transport in single molecular wires’
M.Sc. in Physics, Mooij group, Delft University of Technology, 1993
M.Sc. in Applied Physics, Université Jussieu, Paris, 1991
Positions:
2001–present
Group leader, FOM-Institute for Atomic and Molecular Physics (AMOLF), Amsterdam, NL
2009–present
Professor, Kavli Institute of NanoScience, Bionanoscience department, Delft University of Technology, NL
1999–2001
Postdoctoral research fellow, Carlos Bustamante group, University of California at Berkeley, USA
1999
Postdoctoral research fellow, Cees Dekker group, Delft University of Technology, NL
1998–1999
I.B.M. Netherlands
Practical information
- Informed public
- Free
Organizer
- Profs. Paolo De Los Rios (EPFL-SB, IBI) & Pierre Goloubinoff (UNIL)