Single-molecule protein translocation through nano pores
https://dipc.ehu.eus/en/scientific-activities/joint-seminar-agenda/cic-nanogune/seminar504
https://dipc.ehu.eus/@@site-logo/dipc-logo.png
Single-molecule protein translocation through nano pores
CIC nanoGUNE Seminars
- Speaker
-
Dr. David Rodriguez-Larrea, Dept. of Chemistry, University of Oxford
- When
-
2014/03/24
12:00
- Place
- nanoGUNE seminar room, Tolosa Hiribidea 76, Donostia - San Sebastian
- Add to calendar
-
iCal
Subscribe to Newsletter

Nanopores have emerged as a powerful tool for the analysis of single molecules
in solution. The ionic current passed through them is disrupted by analytes in
a characteristic and measurable way. Protein nanopores offer high
reproducibility in pore dimensions and the ability to introduce site-specific
chemical modifications. This has led to the use of these systems as a platform
for the study of chemical reactions at the single-molecule level and as an
approach towards ultra-fast and cheap sequencing of DNA.
Here I will describe a nanopore system that allows tracking protein co-
translocational unfolding at the single-molecule level. Several biological
processes require protein translocation through narrow pores. For example, the
traffic of proteins across membranes is frequently mediated by them.
Furthermore, the proteasome along with chaperones from the AAA+ family unfold
proteins by pulling them through a narrow pore. Our single-molecule
measurements give insight on how proteins unfold through pores and refold
after translocation.
Protein function, on the other hand, is often regulated by chemical
modifications of specific residues (i.e. post-translational modifications).
Based on the ability of nanopores to detect sequence features I will show that
single-molecule and site-specific detection of post-translational
modifications is feasible.