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Membrane protein structure determination has advanced rapidly in the past years with 500+ structures now in the Protein Data Bank. However the majority of the membrane protein structures are monomeric or form homo-oligomers. Multi-subunit membrane protein complexes are particularly challenging, and comprise only a small fraction of available structures. Yet most membrane proteins exist in complexes rather than isolated entities (Zorman 2015).
Respiratory illness is the 3rd top cause of death as reported by the WHO, a situation that may become even more acute with the rise of antibiotic resistance. Our lab has several projects pertaining to antimicrobial resistance in bacterial respiratory pathogens involving mechanisms facilitated by complex membrane proteins. We have so far expressed and structurally characterised individual or partial components and are now focusing our efforts on obtaining full functionally intact membrane complexes. Towards this goal we have already initiated high-throughput cloning and small scale expression/purification screening experiments involving hundreds of DNA constructs.
The student will be tasked with following up the positive results from these experiments. In the first instance the student will test for complexes in a calibrated fluorescence size exclusion system using technology pre-existing in our lab. An obvious direction is to screen for complex preservation against a panel of detergents. Of particular interest here are a new class of mild detergents (MNGs) and non-detergents such as amphipols and nanodisc techniques reputed to maintain complex integrity. If successful the scale up expression and purification will be performed towards the aim of obtaining a full complex and progressing this into structural studies by X-ray crystallography and electron microscopy.
Suitable Subjects: Biology, Chemistry, Biochemistry
Project duration: 12 weeks
TO APPLY PLEASE FOLLOW THE LINK BELOW
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