Functional Characterisation of insect nicotinic Acetylcholine Receptors
Proteomics/Mass Spectrometry, Department of Biochemistry, University of Cambridge, Cambridge.
This post represents an outstanding opportunity for a protein biochemist to join a multi-disciplinary team working as part of a BBSRC Industrial Partnership Award involving the Departments of Biochemistry and Genetics in Cambridge and Syngenta Jealott's Hill International Research Centre in Berkshire. Despite their importance as major insecticide targets and critical regulators of insect neurophysiology, we know little about the roles that different subunits of nicotinic Acetylcholine Receptors play in their function. A better understanding of these roles is key to more rational design of safe and effective next generation insecticides. We aim to elucidate the role of nicotinic Acetyl Choline Receptor (nAchRs) subunits within receptors and resulting heterogeneity of receptor complexes using a combination of genome editing, membrane proteomics, ligand binding assays and molecular modelling to facilitate rational design of more selective insecticides.
The groups of Prof. Kathryn Lilley (Biochemistry) and Prof. Steve Russell (Genetics) are keen to employ a post-doctoral researcher to work to characterise the nAChRs from Drosophila using cutting edge membrane proteomics tools, building on tools developed by both groups (1,2) and at Syngenta, along with novel technology created by the Dafforn group at the University of Birmingham (3). We are seeking a candidate with experience in quantitative membrane proteomics, and mass spectrometry. Experience in computational proteomics, ligand binding assays and Drosophila biology is also desirable.
Refs: 1. Analysis of the expression patterns, subcellular localisations and interaction partners of Drosophila proteins using a pigP protein trap library. Lowe N et al. Development. 2014 1(20):3994-4005. doi: 10.1242/dev.111054 2. Analysis of Drosophila melanogaster proteome dynamics during embryonic development by a combination of label-free proteomics approaches. Fabre B, et al Proteomics. 201614 (15-16):2068-80. doi: 10.1002/pmic.201500482 3. A method for detergent-free isolation of membrane proteins in their local lipid environment. Lee SC, et al, Nat Protoc. 2016 11(7):1149-62. doi: 10.1038/nprot.2016.070
Fixed-term: The funds for this post are available for 36 months in the first instance.
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