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Computational Enzyme Design for the Development of Biotechnology to Create a new generation of living buildings (Ref: ET20/HLS/APP/SINGH)

  • Full or part time
  • Application Deadline
    Friday, May 08, 2020
  • Funded PhD Project (European/UK Students Only)
    Funded PhD Project (European/UK Students Only)

Project Description

This PhD project will involve the following topics:

• Plastic breakdown: Computational enzyme design to suggest mutants which may improve the catalytic efficiency of PETase and MHETase for polyethylene terephthalate hydrolysis.
• Biomass degradation: Computational enzyme engineering using the directed evolution approach to improve the turnover of the hydrolytic enzyme such as cellulose, lipase and peptidases to improve biomass degradation.

We are seeking an exceptional candidate with background in Chemistry, Biochemistry, Theoretical chemistry, Pharmacy or Pharmaceutical sciences to join the world’s first Hub for Biotechnology in the Built Environment (HBBE, http://bbe.ac.uk/). This is a £8M initiative between Northumbria and Newcastle Universities funded by Research England. The Hub will develop biotechnologies to create a new generation of buildings which are responsive to their environment, grown using engineered living materials, metabolise their own waste, and modulate their microbiome to benefit human health. The Hub is a strategic expansion that will soon including 13 new academic staff, including Biologists, Architectural Designers and Engineers, supported by 5 PDRAs, 14 PhD students and 3 support staff. This will include 3 new research facilities that will integrate our research: the Micro Bio-Design Lab (Northumbria), the Macro Bio-Design Lab (Newcastle) and a unique Experimental ‘Living’ House, ‘The OME’.

The PhD candidate will be based at University of Northumbria, Newcastle upon Tyne, England. This is an excellent opportunity to develop skills in the following; (1) molecular docking, (2) molecular dynamics (MD) simulations, (3) quantum mechanics/molecular mechanics (QM/MM) (4) enhance sampling techniques for the development of novel biocatalysts for biotechnological applications. The computationally predicted mutations will be tested experimentally by the molecular biologist at the HBBE.

The PhD student will also have the opportunity to work in a multidisciplinary team of organic chemist, bioinformatics, molecular biologist and engineers. The PhD student will have the opportunity to attend national and international conferences and will be sent to specialized workshops to obtain necessary skills for the successful completion of the PhD project.

Eligibility and How to Apply:
Please note eligibility requirement:
• Academic excellence of the proposed student i.e. 2:1 (or equivalent GPA from non-UK universities [preference for 1st class honours]); or a Masters (preference for Merit or above); or APEL evidence of substantial practitioner achievement.
• Appropriate IELTS score, if required.

For further details of how to apply, entry requirements and the application form, see
https://www.northumbria.ac.uk/research/postgraduate-research-degrees/how-to-apply/

Please note: Applications should include a covering letter that includes a short summary (500 words max.) of a relevant piece of research that you have previously completed and the reasons you consider yourself suited to the project. Applications that do not include the advert reference (e.g. ET20/…) will not be considered.

Deadline for applications: 8th May 2020
Start Date: 1st Aug 2020

Northumbria University takes pride in, and values, the quality and diversity of our staff. We welcome applications from all members of the community. The University holds an Athena SWAN Bronze award in recognition of our commitment to improving employment practices for the advancement of gender equality.

For informal enquiries please contact Dr Warispreet Singh ()

Funding Notes

The studentship is available to Home and EU students with a full stipend, paid for three years at RCUK rates (for 2020/21, this is £15,285 pa) and full Home/ EU Fees.

References

1. Xu, J., Cen, Y., Singh, W., Fan, J., Wu, L., Lin, X., Zhou, J., Huang, M., Reetz, M. T., and Wu, Q. (2019) Stereodivergent Protein Engineering of a Lipase to Access All Possible Stereoisomers of Chiral Esters with Two Stereocenters. J. Am. Chem. Soc. 141, 7934–7945.

2. Cen, Y., Singh, W., Arkin, M., Moody, T., Huang, M., Zhou, J., Wu, Q., and Reetz, M. (2019) Artificial Cysteine-Lipases with High Activity and Altered Catalytic Mechanism Created by Laboratory Evolution. Nat. Comm. 10, 3198.

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