About the Project
Myoglobin, the oxygen-binding protein in muscle, is a prototype for developing haem-based oxygen carriers. The problem of myoglobin production in recombinant expression systems is that the protein tends to form non-functional and even dangerous aggregates at the high concentrations required for industrial production.
Research at Liverpool has revealed that myoglobin in diving mammals and birds has special properties that allow it to maintain its stability and proper function at much higher cellular concentrations than in terrestrial mammals. See: https://www.youtube.com/watch?v=vjk6e3kSNuY
The aim of this project is to determine the molecular mechanism(s) behind the increased stability and maximal concentration of myoglobin in diving animals and to use this knowledge for the development of an improved oxygen carrier. This project provides multi-disciplinary training in bioinformatics and genomics, biochemical and biophysical techniques and evolutionary physiology and ecology.
For further information see the website: https://www.liverpool.ac.uk/integrative-biology/
The project is suited to a student with at least a good B.Sc. Upper Second in Biological or Life Sciences (particularly Biomedicine, Biochemistry, Molecular Biology, Bioinformatics, or Comparative Physiology).
Assistance will be given to applications who are applying to international funding schemes.
The successful applicant will be expected to provide the funding for tuition fees and living expenses as well as research costs of £3.000 per year.
A fee bursary may be available for well qualified and motivated applicants.
Details of costs can be found on the University website: https://www.liverpool.ac.uk/study/postgraduate-taught/finance/#living-expenses
The work is show-cased in a video featured on the BBSRC website: http://webarchive.nationalarchives.gov.uk/20160108075453/http://www.bbsrc.ac.uk/news/health/2013/130614-pr-study-diving-mammals-underwater-endurance/
Davies H.A., Madine J., Middleton D.A. (2015). Comparison with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid polypeptide medin, The Journal of Biological Chemistry 290: 7791-7803
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