| Qualification Type: | PhD |
|---|---|
| Location: | Falmer |
| Funding for: | UK Students |
| Funding amount: | UKRI rate (London weighting), and a consumables budget |
| Hours: | Full Time |
| Placed On: | 5th March 2026 |
|---|---|
| Closes: | 3rd April 2026 |
Funding for: UK Students
Funding amount: Funding will cover tuition fees for UK students (at the Home rate), a stipend at the UKRI rate, and a consumables budget.
This is a 3.5-year PhD studentship funded by the School of Life Sciences and Diamond Light Source, starting on 1st October 2026
This PhD project offers a unique opportunity to join a highly interdisciplinary team at the forefront of drug discovery and structural biology. The research focuses on elucidating the complex structural architecture of essential regulatory proteins, including kinases, which play critical roles in maintaining cellular homeostasis and driving cancer progression. Many of these pivotal proteins currently lack high-resolution experimental structural data, creating a significant knowledge gap that hinders the global development of targeted therapies. By filling this gap, the project aims to identify and validate promising novel chemical scaffolds to support the creation of potent, specific modulators for advanced mechanistic studies and future therapeutic applications.
As a doctoral candidate in this program, you will be fully embedded within a collaborative network involving leading experts from the Sussex Drug Discovery Centre at the University of Sussex and Diamond Light Source. This role involves spending approximately 50% of your total studentship based at the national synchrotron facility, providing a unique immersion in a world-leading research environment. You will work directly alongside structural biologists, biophysicists, and medicinal chemists to bridge the existing gap between fundamental molecular science and translational medicine.
Central to this project is the development of a novel platform for drug discovery combining Synchrotron Radiation Circular Dichroism (SRCD) with XCHEM fragment screening. This innovative, high-throughput approach will allow for the rapid identification of small-molecule binders while simultaneously providing detailed insights into secondary and tertiary structural rearrangements and ligand-induced conformational changes. You will integrate this platform with X-ray Crystallography and Cryo-Electron Microscopy (Cryo-EM) to determine high-resolution, atomic-level structures of protein domains and their complexes. Furthermore, you will utilize BioSAXS to study solution-state conformations, flexibility, and various oligomeric states.
Through this combination of techniques, you will gain a robust, comprehensive toolkit and interdisciplinary expertise essential for a professional career in the modern pharmaceutical industry or academic structural biology.
For enquiries about the project, please email Erika Mancini (e.mancini@sussex.ac.uk) or John Spencer (j.spencer@sussex.ac.uk)
References:
https://www.sussex.ac.uk/research/centres/sussex-drug-discovery-centre/
https://www.diamond.ac.uk/Instruments/Soft-Condensed-Matter/B23.html
https://www.diamond.ac.uk/Instruments/Soft-Condensed-Matter/B23/Staff/Hussain.html
Eligibility & How to apply:
Please submit a formal application using the online admissions portal attaching a CV, degree transcripts and certificates, and two academic referees. A research proposal is not required. Instead, upload a personal statement describing your interests, skills, previous experience, and why you are applying to this project.
On the application system select Programme of Study – PhD Biochemistry. Please select ‘funding obtained’ and state the supervisor’s name where required.
Candidates must have, or be expected to obtain, a minimum 2:1 undergraduate degree in Biochemistry, Chemistry, Biology or related field. An MSc degree in Structural Biology, Cancer Biology, or Biophysics is advantageous.
Candidates for whom English is not their first language will require an IELTS score of 6.5 overall or equivalent proficiency - English language requirements
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