Oxidative protein folding of industrially and pharmaceutically important recombinant proteins at The University of Manchester on FindAPhD.com

Dr Hui Lu, Dr A Day Applications accepted all year round Self-Funded PhD Students Only

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Manchester United Kingdom Analytical Chemistry Biochemistry Bioinformatics Biophysics Molecular Biology Structural Biology

Faculty of Biology, Medicine and Health, The University of Manchester

About the Project

Oxidative protein folding (protein folding and disulphide bond formation) is important for function and stability of many proteins. Disulphide bond formation is one of the most common post-translational modifications found in proteins, which is catalysed by dedicated sulphydryl oxidoreductase systems in specialized cellular compartments (e.g. the ER, mitochondrial intermembrane space) in vivo. Moreover, misfolded disulphide bonds can be reduced (broken) and corrected by disulphide reductases and/or isomerases. Therefore, it is no supervise that oxidative folding of proteins in vitro is challenging and often a key problem of recombinant protein production. In this project, we are interested in study oxidative folding of industrially and pharmaceutically important recombinant proteins, for example, TGF-βs (Transforming Growth Factor beta), and how thiol/disulphide oxidoreductases such as Mia40-Erv1, PDI, and Trx systems affect the folding of these proteins in vitro. The project aims to enhance the oxidative refolding yields of industrially and pharmaceutically important proteins, as well as understanding protein folding mechanisms of the target proteins. The key techniques required for this project include protein expression and purification, protein folding and functional characterisations using electrophoresis, chromatography, and various spectroscopic methods. This project will provide an excellent opportunity for a self-motivated student to learn and develop many essential skills used in protein studies.

Entry Requirements

Candidates are expected to hold (or be about to obtain) a minimum upper second class honours degree (or equivalent) in a related area/subject. Candidates with previous laboratory experience, particularly in cell culture and molecular biology, are particularly encouraged to apply.

How To Apply

For information on how to apply for this project, please visit the Faculty of Biology, Medicine and Health Doctoral Academy website (https://www.bmh.manchester.ac.uk/study/research/apply/). Informal enquiries may be made directly to the primary supervisor. On the online application form select PhD Genetics

For international students, we also offer a unique 4 year PhD programme that gives you the opportunity to undertake an accredited Teaching Certificate whilst carrying out an independent research project across a range of biological, medical and health sciences.

Equality, Diversity and Inclusion

Equality, diversity and inclusion is fundamental to the success of The University of Manchester, and is at the heart of all of our activities. The full Equality, diversity and inclusion statement can be found on the website https://www.bmh.manchester.ac.uk/study/research/apply/equality-diversity-inclusion/”

For international students we also offer a unique 4 year PhD programme that gives you the opportunity to undertake an accredited Teaching Certificate whilst carrying out an independent research project across a range of biological, medical and health sciences. For more information please visit http://www.internationalphd.manchester.ac.uk

Funding Notes

This project is offered as a one year MPhil or a three year PhD. Applications are invited from self-funded students. This project has a Band 2 fee. Details of our different fee bands can be found on our website (View Website).

As an equal opportunities institution we welcome applicants from all sections of the community regardless of gender, ethnicity, disability, sexual orientation and transgender status. All appointments are made on merit.

References

Ang SK, & Lu H. (2009) Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p, J Biol Chem. 284, 28754-61.

Gisby MF, Mellors P, et al, & Day A (2011) A synthetic gene increases TGFβ3 accumulation by 75-fold in tobacco chloroplasts enabling rapid purification and folding into a biologically active molecule. Plant Biotechol J 9, 618-628.

Hell K (2008) The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria, Biochim Biophys Acta. 1783, 601-9. Review

Riemer J, Bulleid N & Herrmann JM (2009) Disulfide formation in the ER and mitochondria: two solutions to a common process, Science. 324,1284-7. Review

Spiller MP, Ang SK et al & Lu H (2013) Identification and characterization of mitochondrial Mia40 as an iron-sulfur protein. Biochem J. 455, 27-35.

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