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Life in the freezer – how do proteins function in the cold?


Project Description

Life can be found in almost every environment on Earth including hot thermal springs, highly saline lakes and acidic waterways. Life is also found in cold environments (< 15 °C, e.g. polar environments, at altitude and most of the deep oceans). Organisms adapted to life in the cold (psychrophiles) face a wide range of challenges such as increased solution viscosity, decreased diffusion rates, decreased protein synthesis rates and most importantly the exponentially decreasing rates of reaction with lower temperature. Despite this latter effect, psychrophilic enzymes maintain activity at low temperatures but the mechanism by which this feat is achieved is unclear. The aim of this studentship is to use a wealth of biophysical and biochemical methods to investigate how psychrophilic proteins maintain catalytic activity in the cold – a feat that, if understood, would allow provide great environmental benefit by obviating the need to heat reactions in industrial and domestic applications.

Funding Notes

White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs

Requirements:
At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship

Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.

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References

1. Inducing protein aggregation by extensional flow. Dobson, J., Kumar, A., Willis, L., Tuma, R., R. Higazi, D., Turner, R., Lowe, D., Ashcroft, A., Radford, S., Kapur, N. and Brockwell, D. (2017) Proc Natl Acad Sci USA. 114:4673-4678.
2. Gating of TonB dependent transporters by substrate-specific forced remodeling. Hickman, S., Cooper, R., Belluci, L., Paci, E. and Brockwell, D. (2017) Nature Commun. 8: article no. 14804
3. Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Gruszka,. D., Whelan, F., Farrance, O., Fung, H., Paci, E., Jeffries, C., Svergun, D., Baldock, C., Baumann, C., Brockwell, D., Potts, J. and Clarke, J. (2015) Nat Commun 6: article no. 7271.
4. Disorder drives cooperative folding in a multidomain protein
DT Gruszka, CATF Mendonça, E Paci, F Whelan, J Hawkhead, JR Potts, Clarke, J Proc Natl Acad Sci USA 113 (42), 11841-11846

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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