About the Project
Candidates are expected to hold (or about to obtain) a minimum second class (for MPhil study) and upper second class (for PhD study) honours degree (or equivalent) in biochemistry, cell biology or a related subject. Candidates with experience in protein folding, characterisation, and/or computer modelling, with an interest in protein folding and protein biotechnology are encouraged 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 Biochemistry.
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
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.
Mordas A, Tokatlidis K. The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis. Acc Chem Res. (2015) 48(8):2191-9. Review
Ang SK, Lu H. Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p. J Biol Chem. (2009) 284(42):28754-61.
Guo PC, Ma JD, Jiang YL, Wang SJ, Bao ZZ, Yu XJ, Chen Y, Zhou CZ. Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space. J Biol Chem. (2012) 287(42):34961-9.
Tang X, Ang SK, Ceh-Pavia E, Heyes DJ, Lu H. Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria. FEBS J. (2020) 287:1220-1231.
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