PhD in Protein Binder Design and DNA Damage Response Research: The Wu Lab at the University of Leeds has announced a fully funded PhD studentship through the competitive, worldwide BBSRC Yorkshire Bioscience Doctoral Training Partnership.
The project is co-supervised by Dr Qian Wu and Dr Richard Bayliss, with the focus on designing next-generation protein binders that target essential components of the DNA damage response network.
For students passionate about structural biology, protein engineering, or molecular mechanisms that protect genome integrity, this is a standout opportunity.
Why Pursue a PhD at the University of Leeds?
Fully Funded Support: Through the BBSRC Yorkshire Bioscience DTP, the position covers full tuition for eligible students worldwide, a competitive stipend, and research training support.
Research Area: The proposed project will develop protein binders that selectively bind and regulate essential DNA damage response (DDR) proteins.
Advanced Training: Students will get to know how to design protein interactions with high-tech equipment, assess the performance of the binder and combine multidisciplinary methods into their work.
Effective Mentorship and Cooperation: Dr Qian Wu and Dr. Richard Bayliss are its joint supervisors. Students will also be provided with regular research advice, career development assistance, and the possibility to collaborate.
Vibrant Lab Culture: At the Wu Lab, selected students will join a supportive environment where mentorship comes from both faculty and peers, and where research progress is celebrated together.
Position Description – PhD in Protein Binder Design and DNA Damage Response Research
The proposed PhD project will apply the latest de novo protein design to develop new tools capable of targeting and modulating DDR proteins in a specific fashion. It focuses on the discovery of DDR proteins functionality and interaction, which brings new information to the maintenance of the genome and prevention of diseases.
The research group will recruit the chosen PhD student to the Wu Lab and use sophisticated computational methods to create protein binders, which will undergo biochemical and structural characterisation to determine their specificity and functionality in cells.
Moreover, the student will also compare the effect on the DDR protein interactions that can modulate the DNA repair and cellular response to DNA damage.
The results of this project would not only improve the knowledge of the stability of the genome, but also would ensure a future treatment approach to cancer and other diseases associated with the instability of the genome.
Qualifications for the PhD Studentship
Applicants should have a strong academic record, at least an upper second-class honours degree or equivalent.
Must have a solid background in any biological, chemical, or physical science or mathematics field (such as biochemistry, molecular biology, structural biology, bioengineering, etc.)
Applicants may need to provide evidence of their English language ability. Refer to the English language requirements for the host university
Show interest or experience in protein engineering, computational modeling, DNA repair pathways, or structural techniques.
Have strong communication skills and enthusiasm for collaborative research.
Applicants from all backgrounds can apply, regardless of age, ethnicity, gender, gender identity, disability, sexual orientation, or career pathway to date.
International students should check if they meet the entry requirements for the host university.
Application Process – PhD in Protein Binder Design and DNA Damage Response Research
The application process involves completing and submitting an Expression of Interest form. You can apply for up to two YBDTP projects (which may be at separate universities).
In addition, you may be required to provide the following documents: a CV, academic transcripts, a personal statement, and references.
Deadline and Contact Information
Application Deadline: January 7, 2026
Send an email to the project supervisor via email if you have any questions about the project, or visit the official program’s web page (click here).