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Research Assistant in Biological Chemistry
Cardiff School of Chemistry
We seek to recruit an enthusiastic, highly motivated scientist with proven intellectual and technical abilities to work on a Biotechnology and Biological Science Research Council (BBSRC)-funded biological chemistry project.
The overall objective of this research project is to characterise the protein electrostatic properties of Dihydrofolate reductase (DHFR) via vibrational Stark effect measurements via incorporation of cyanide probes into a protein to reveal subtle electrostatic changes within the protein microenvironment (Stark effect).
Applicants must hold a 2:1 or 1st Class Honours degree (or equivalent) in Biological/Organic Chemistry or Biochemistry especially relative to Synthetic Biology, or equivalent industrial experience.
Further information is available at http://www.cardiff.ac.uk/people/view/38538-allemann-rudolf .
For informal enquiries about the role and the School of Chemistry, please contact Professor Rudolf Allemann (AllemannRK@cardiff.ac.uk; 02920 688443).
For further details about working at Cardiff University, please contact Ms Alison Blake (BlakeAF@cardiff.ac.uk; 02920 874805).
This position is full time (35 hours per week) and is available immediately for a year.
Salary: £26,495 - £30,688 per annum (Grade 5)
Important note: It is the University’s policy to use the person specification as a key tool for short-listing. Candidates should evidence that they meet ALL of the essential criteria as well as, where relevant, the desirable. As part of the application process you will be asked to provide this evidence via a supporting statement. Please ensure that the evidence you are providing corresponds with the numbered criteria outlined below. Your application will be considered based on the information you provide under each element.
When attaching the supporting statement to your application profile, please ensure that you name it with the vacancy reference number, e.g. Supporting Statement for 6503BR.
Please be aware that Cardiff University reserves the right to close this vacancy early should sufficient applications be received.
Cardiff University is committed to supporting and promoting equality and diversity and to creating an inclusive working environment. We believe this can be achieved through attracting, developing, and retaining a diverse range of staff from many different backgrounds who have the ambition to create a University which seeks to fulfil our social, cultural and economic obligation to Cardiff, Wales, and the world. In supporting our employees to achieve a balance between their work and their personal lives, we will also consider proposals for flexible working or job share arrangements.
To contribute to research in the area of Biological Chemistry, carrying out supporting work that helps lead to the publishing of research in high-quality journals. To pursue excellence in research and to inspire others to do the same.
Main Duties and Responsibilities
Qualifications and Education
Knowledge, Skills and Experience
Communication and Team Working
This project aims to investigate the nature of protein electrostatics in Dihydrofolate reductase (DHFR) catalysis. The underlying role of protein electrostatics in enzyme catalysis needs to be deciphered in order to build a precise model for DHFR catalysis. We hypothesise that enzymes need to sample an electrostatically preorganised configuration to find the best configuration for the reaction to occur. Accordingly, both protein dynamics and electrostatics need to be characterised. Here we will characterise the protein electrostatic properties of DHFR via vibrational Stark effect measurements. Incorporating a cyanide probe into a protein reveals a unique infrared (IR) signal, the changes of which caused by amino acid replacement and/or ligand binding can reveal subtle electrostatic changes within a protein microenvironment, hence vibration Stark effect. Natural aromatic residues in the active site will be replaced by commercially available unnatural amino acid such as cyanylated phenylalanine using the aminoacyl transfer ribonucleic acid (tRNA) synthetase variant made available in our laboratory from previous work. Ligand binding will lead to a strong different in the measured vibration Stark effects, The IR spectroscopic measurement will be combined with site-directed mutagenesis studies to investigate the roles of catalytically important residue in catalysis. To confirm our experimental results, vibrational Stark effects will also be performed computationally with collaborators.