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Distinguished iNANO Lecture: Single-Molecule Protein Translocation Through Nanopores

Dr. David Rodriguez-Larrea, Bayley Research Group, University of Oxford, United Kingdom

Info about event


Friday 7 March 2014,  at 10:15 - 11:00


The auditorium of the iNANO House (1593-012), Gustav Wieds Vej 14, 8000 Aarhus C


Dr. David Rodriguez-Larrea, Hagan Bayley Research Group, University of Oxford, United Kingdom

Single-Molecule Protein Translocation Through Nanopores

Nanopores have emerged as a powerful tool for the analysis of single molecules in solution. An ionic current passing through the pore 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 platforms 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 lipid membranes and, 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.

Hosts: Professor Kurt Gothelf & PhD student Christian Bech Rosen, iNANO, CDNA & Dept. of Chemistry, Aarhus University, Aarhus, Denmark


Coffee, tea and bread will be served in front of the iNANO auditorium from 10:00.