We are a chemical biology group which focuses on protein chemistry, molecular genetics and biophysics. Much of our work is centered on membrane proteins, in particular channels and pores. We are currently investigating both the fundamental properties of these proteins and their applications in biotechnology.
Several of our studies are collaborations with other laboratories in the UK, USA and Europe. There are currently 14 postdocs, 8 graduate students and a technician in the laboratory, from 12 different countries.
News from the Lab:
- We welcome postdocs Jianwei Li and Nobina Mukherjee to the group!
- New postdoc positions available. Joint projects between the Kleanthous, Bayley and Robinson groups. We are seeking to appoint 2 postdocs with complementary skills in biochemical and biophysical dissection of membrane protein complexes to study the newly discovered process of intrinsically disordered protein (IDP) translocation through bacterial porins. The posts are part of a collaborative research programme involving the laboratories of Colin Kleanthous in the Department of Biochemistry and Hagan Bayley and Carol Robinson in the Department of Chemistry. More information on the posts can be found here: Link
- Congratulations to Mariam Ayub who won the Analytical Methods award at the recent Gordon Research Conference - Bioanalytical Sensors meeting.
- Congratulations to Ivan Dimov who won the Part II Chemical Biology prize for his final year dissertation.
- Financial Times article- ‘Cheap DNA sequencing will transform medical research’ highlights Oxford Nanopore’s MinIon.
- 2x Chemical Biology PDRA positions available in our group. Further details can be found here. Vacancy ID: 113622. c/d 03-July-2014
- Our new paper entitled ‘Single-molecule analysis of chirality in a multicomponent reaction network’ has been published in Nature Chemistry. The paper describes the use of the αHL nanoreactor approach to study multicomponent substitution reactions of arsenic(II) compounds with thiols, thus stretching the limits of the protein pore technology for the analysis of dynamic systems.