Postdoctoral Research Associate in the Molecular Biology of Carbon Dioxide Sensing

Durham University; North East; On-site; GBP 30,000 - 40,000; Full time

Job summary

Durham University offers a fixed-term research position focused on identifying carbon dioxide-binding proteins. This role provides an exciting opportunity to develop interdisciplinary skills in biosciences and physical sciences, contributing to groundbreaking research in understanding carbon dioxide's biological interactions.

Qualifications

• Experience in molecular biology techniques.
• Familiarity with protein analysis methods.
• Ability to work collaboratively in research settings.

Responsibilities

• Identify carbon dioxide-binding proteins.
• Collaborate with colleagues at Warwick University.
• Conduct research on molecular responses to carbon dioxide.

Skills

Interdisciplinary skills

Research in biosciences

Analytical skills

Education

PhD in a relevant field

Job description

The Role

The identification of carbon dioxide-binding proteins

Carbon dioxide is essential for life. It is at the beginning of every life process as a fundamental substrate of photosynthesis or chemosynthesis and is at the end of every life process as the product of aerobic respiration and post-mortem decay. As such, it is not a surprise that this gas regulates such diverse processes as cellular chemical reactions, transport, maintenance of the cellular environment, behaviour, and immunity. Carbon dioxide is a strategically important research target with relevance to crop responses to environmental change, insect-borne disease, and public health. However, we know very little of the direct interactions of carbon dioxide with the cell, despite the importance of the gas to biology.

Carbon dioxide mediates the earliest known example of a protein post-translational modification (PTM), identified on haemoglobin in 1928. It can directly combine with select protein groups to form carbamates. Influential research from the 1920s-80s demonstrated that the carbamate PTM regulates oxygen-binding in haemoglobin and activates the carbon dioxide-fixing enzyme Rubisco. George Lorimer proposed carbamate PTMs as a mechanism for regulating biological responses to carbon dioxide in 1983. However, the carbamate PTM is unstable outside the cell, and its identification presents significant analytical challenges. Several stable carbamates have been identified in protein structures, but technical difficulties have limited their widespread recognition, and carbon dioxide-mediated carbamylation is largely overlooked as a PTM. For instance, the Wikipedia page for PTM does not mention carbon dioxide-mediated carbamylation among the 61 identified PTMs.

Direct protein targets for carbon dioxide sensing are almost entirely unknown. We have developed technology to systematically identify carbon dioxide-binding proteins. We aim to understand how insect chemosensory receptors can sense and respond to carbon dioxide. This research will provide broad insights into molecular responses to carbon dioxide and develop tools that will revolutionize our understanding of its biology. The work will be conducted in collaboration with colleagues at Warwick University.

This position offers an exciting opportunity to develop interdisciplinary skills in biosciences and physical sciences in a novel area of biology.

The post is fixed-term for 6 months, and the successful candidate will work with Prof. Martin Cann (PI; Dept of Biosciences) at Durham University.