Post-doctoral vacancies in the Ultrafast group:


None currently available


PhD Studentship Openings in the Ultrafast group:


3.5 yr PhD studentship in Ultrafast Chemical Physics

Monitoring Biological Transformations in Real Time with Ultrafast 2D-IR Spectroscopy

Applications are invited for a fully-funded 3 ½ year PhD studentship in the group of Dr Neil Hunt at the University of Strathclyde (Dept of Physics). The aim of the project is to apply novel multidimensional ultrafast infrared spectroscopy methods to understand the role that protein structural dynamics play in biological reactions; ultimately we aim to observe biological reactions spectroscopically in real time.

The Strathclyde Multidimensional Spectroscopy group are currently funded by grants totalling over £2.2M and occupy a suite of newly-refurbished laboratories. Our research work is inherently cross-disciplinary with many of our projects occurring at the Physics and Life Sciences interface and all of them containing an element of collaboration. This studentship will complement existing projects in the group and would suit an ambitious and motivated candidate with a first degree in physics or chemistry with an interest in learning the new skillset that accompanies multidisciplinary research, no previous biological experience is necessary but would be an advantage. The fully-funded studentship is open to EU citizens only.

Further details: It is well-known that the structure of proteins influences their functionality. However, biological molecules are far from static and their structure fluctuates rapidly on timescales from picoseconds (one millionth of a millionth of a sec) to nanoseconds (billionth of a sec) and slower. These fluctuations must play a key role in controlling the mechanisms of biological reactions though little is known about the specific way in which these reactions proceed and the tools required to probe these dynamics have not been available. Ultrafast time resolved 2D-IR spectroscopy is a new technique that combines the structural insights of infrared spectroscopy with the time resolution required to observe the structural fluctuations of proteins. The aim of this project is twofold; firstly to apply 2D-IR spectroscopy to examine the structural dynamics of proteins and secondly, to develop new methods to enable observation of biological reactions in real time with 2D-IR. The project will build on preliminary data (Hunt et al, Biochem J, 2011, v433, p459) using 2D-IR spectroscopy to interrogate the fluctuations of NO sensing proteins. NO is an important biological molecule that is vital to both bacterial and mammalian biology and understanding its interactions with biological systems is considered one of the important questions facing modern biological research. This project will form part of a large collaborative effort including the Strathclyde Institute of Pharmacy and Biomedical Science, Diamond Light Source Ltd and the STFC Rutherford Appleton laboratory; as such opportunities exist for the successful candidate to engage in collaborative visits to these project partners for experimental work associated with the studentship.

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