Postdoctoral Research Scientist (Signalling)
Babraham Institute, UK
Application Deadline: Monday 5th January 2026
We are seeking an enthusiastic and talented Postdoctoral Research Scientist to join the David group at the Babraham Institute in Cambridge. Our overarching goal is to discover mechanisms that promote healthy ageing and alleviate age-related diseases such as Alzheimer’s disease. Our group has uncovered mechanisms that prevent age-related protein aggregation, a major contributor to functional decline. Notably, we discovered a proteostasis network that safeguards proteins from aggregation in the extracellular space in C. elegans (PMID: 32641833). Our group is embedded within the Signalling Programme, which offers a vibrant, collaborative environment and access to world-class facilities.
In this role, you will have the opportunity to develop an independent research project investigating mechanisms of protein quality control in the extracellular space. Your work will combine in vitro assays to characterize protein aggregation and in vivo studies in C. elegans using imaging, proteomics, and functional assays to explore how extracellular proteostasis influences organismal health. This position is ideal for a curiosity-driven scientist who thrives on tackling challenging questions and pushing the boundaries of knowledge.
Postdoctoral Research Scientist (Signalling) job - Babraham Institute - Babraham Institute
Deconvoluting the sequence determinants for outer membrane protein folding, stability and function
University of Leeds, UK - PhD
Start Date: Thursday 1st October 2026
Application Deadline: 5pm on Wednesday 7th January 2026
The cell walls of Gram-negative bacteria are packed with b-barrel outer membrane proteins (OMPs) that are essential for bacterial growth and virulence. Targeting OMP biogenesis is thus a potential route to combat antibiotic resistance. OMPs are also attractive as nanoscale sensor and sequencing scaffolds. Exploiting these opportunities is currently not possible due to our poor understanding of (i) how OMPs are transported and maintained in a folding competent state from their synthesis to their folding and insertion into the outer membrane and (ii) how the protein sequence affects OMP structure and stability. This lack of understanding is due to the paucity of data on the effects of mutation on the expression, stability and function of OMPs. Here, we will address these questions using deep mutational scanning (DMS). DMS uses an in vivo fitness screen to link the phenotype of a bacteria to its genotype. Monitoring the change in abundance of each variant by next generation sequencing upon increasing the selective pressure on the bacteria allows quantification of variant fitness. In this way, the effect of thousands of sequence variants can be measured without prior expression and purification. We have previously used this approach to quantify the effects of 750 variants of the culprit protein in Alzheimer’s disease (https://doi.org/10.1073/pnas.2516165122) and to develop better biopharmaceuticals (https://www.nature.com/articles/s41467-020-15667-1). In this exciting multi-disciplinary project, you will use a wide range of techniques and approaches spanning molecular biology, biochemistry, biophysics and computational biology, to (i) Deliver new fundamental understanding of the design principles of OMP sequences for efficient folding in vitro; and (ii) Enable new understanding of sequence and structural motifs that enable efficient folding of OMPs in vivo. The outcome will be new fundamental knowledge of sequence-structure relationships in OMP folding and the translation of this knowledge for benefits in biotechnology and medicine.