School of Biological Sciences

Scholarships and funding

Supporting your studies

We offer funding opportunities to support both undergraduate and postgraduate students, including a broad range of University of Essex scholarships, and postgraduate research studentships within the School and from ARIES DTP.

Scholarships

Our range of scholarships and bursaries to support talented students ensure we remain accessible to all with the potential to succeed, regardless of financial circumstances.

Search our Scholarship Finder to see the funding you can apply for.

University of Essex Doctoral Scholarships

Our University of Essex Doctoral Scholarships support talented PhD students pushing boundaries in their field of study.

Applications for 2018-19 funding have closed. Funding news for 2019-20 will be available in due course.

MSD studentships - The Christine Desty Scholarship

Christine Desty was a talented chemist, graduating from Essex with a BSc Biochemistry in 1975. Sadly, she passed away a few years later. Her mother Doreen, the wife of the late scientist and inventor Denis Desty, chose to pay tribute to her daughter by setting up a Scholarship fund in the School of Biological Sciences. The fund will create 10 MSD scholarships in the School, generating a next generation of talented Essex scientists.

The Christine Desty Scholarship is fully-funded (Home/EU fees £4630 plus stipend of £15,009) for an MSc by Dissertation (MSD) in the School of Biological Sciences, University of Essex.

If you have any queries about the scholarship or online application process please contact Emma Revill (ecrix@essex.ac.uk)

Creating the next generation LPMOs for biofuel production

Deconstructing plant and non-plant (e.g. fungal) biomass to value added products will become a major route to obtain sustainable materials in many industrial processes like food, feed manufacturing, non-food and renewable bioenergy.

A significant proportion of the polysaccharides in biomass resists deconstruction with the currently available enzyme cocktails for cellulose, chitin and starch. New enzymes and/or improved versions of existing enzymes will be needed to include this fraction of the biomass to the product stream. This project is concerned with the latter and is focused on a family of copper (Cu) containing enzymes called lytic polysaccharide monooxygenases (LPMOs).

These enzymes are now known to perform the oxidative pre-treatment of the biomass to make it readily available for further breakdown by hydrolases such as cellulases and amylases.

In collaboration with a German company, WeissBioTech, Leiden University (Netherlands) and funded through a BBSRC Business Interaction Voucher we have developed an in vivo library screen for a AA13 starch LPMO with the goal to identify better performing LPMOs and test whether these can be used in industrial starch liquefaction. Libraries are based on a series of loops that create an active surface for substrate interaction surrounding the active site Cu.

By re-engineering these loops through creation of synthetic loop-saturation-libraries and screening in a Streptomyces host, ‘winners’ i.e. a better performing AA13 LPMO variants with enhanced substrate activity, can be identified.

Work plan

The MSD student will work towards meeting the following objectives:

  • Create expression constructs for heterologous production of AA13 LPMO ‘winners’ identified from the in vivo screen using established methods. (months 1-3)
  • Purify and characterise the ‘winners’ using structural (X-ray crystallography) and biophysical techniques (differential scanning fluorimetry). (months 3-12)
  • Test the purified ‘winners’ during a secondment at WeissBioTech, Zwingenberg, using their Brabender Viscograph apparatus for assaying liquefaction. (month 8)

Applying

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Jonathan Worrall (jworrall@essex.ac.uk) and Dr Mike Hough (mahough@essex.ac.uk)

Closing date: 24 April 2019

Effect of oxidative stress on the biochemistry of dimethylsulfoniopropionate (DMSP)-lyase enzymes in tropical reef organisms

Tropical coral reefs are a substantial source of the climate-cooling gas dimethyl sulfide (DMS). The major precursor of DMS is the secondary metabolite dimethylsulfoniopropionate (DMSP) that is biosynthesised to high concentrations in symbiotic dinoflagellates of the tropical genus Symbiodinium.

In the phytoplankton Emiliania huxleyi, the algal Alma DMSP-lyase enzymes are responsible for the production of DMS and Symbiodinium contains homologs of Ehux-Alma1.

Despite their global importance, the biochemical function of DMSP and DMS in corals is underexplored. Since both operate as antioxidants that scavenge harmful reactive oxygen species (ROS) in E. huxleyi, the cycling of DMSP and DMS may have profound implications for the susceptibility of corals to ROS-induced lethal coral bleaching and the following destruction of reef environments.

Supported with an ongoing PhD project and in collaboration with King Abdullah University of Science and Technology (KAUST), we recently started building understanding of the dynamics of DMSP and DMS in the Aiptasia-Symbiodinum model system under physiological stress. Importantly, we grow Aiptasia-Symbiodinum combinations that show different susceptibilities to ROS-induced bleaching making this model system a preferred choice to study the function of DMSP/DMS under oxidative stress.

The studentship applied for here will align with our ongoing efforts by investigating the biochemical basis of DMSP-to-DMS conversion in Symbiodinium and Aiptasia.

With guidance from the supervisors, the student will direct the project’s research emphasis and develop scientific hypotheses to assess the function of DMSP and DMS in the Aiptasia-Symbiodinum model system.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Michael Steinke (msteinke@essex.ac.uk), Dr Mike Hough (mahough@essex.ac.uk) and Dr Jonathan Worrall (jworrall@essex.ac.uk)

Closing date: 24 April 2019.

Exploring the role of human cytoglobin in cancer therapy resistance

A series of new haemoglobins have been discovered over the past 20 years including a ubiquitously expressed vertebrate protein, cytoglobin. Although with a similar structure to the well characterised blood haemoglobin, this globin does not function as a classical oxygen carrier. Thus the physiological functions of this protein remain largely unknown. However, there has been a realisation of the importance of cytoglobin in the mechanism of cancer development and cancer therapy resistance. For example, cytoglobin-deficient mice have been found to have increased risk of cancer development in the lungs and liver when exposed to carcinogens1.

Additionally, increased expression of cytoglobin correlates with a tumour’s agressiveness2 and could potentially be a new biomarker for cancer. Therefore, we wish to study the mechanism of how cytoglobin protects tumours and in doing so identify potential new targets against cancer therapy resistance. 

We have previously investigated the various potential physiological and pathological roles of human cytoglobin through in vitro biochemical techniques3,4. We are now in a position to utilize our understanding of the biochemistry of cytoglobin to assess its role in cytoprotection under various stress conditions such as hypoxia, oxidative stress and nitrative stress and to investigate its role in cell signalling.

The aims of this studentship are to explore the characteristics of human cytoglobin and how these may relate to protection of cells against stress mechanisms within the cell and hence give valuable new insights into the role of cytoglobin in cancer therapy resistance.

The project involves generation and study of cytoglobin and specific mutations in cancer cell lines through CRISPR/Cas9 gene editing, transient expression, stably transfected cell lines, and gene silencing. In this way known key functional amino acids of cytoglobin will be targeted and changes in the reactivity of the protein will be mapped to changes in cell stress response. In addition, in situ techniques will be used to correlate changes in the cell redox environment to changes in protein redox state.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Brandon Reeder (reedb@essex.ac.uk) and Dr Greg Brooke (gbrooke@essex.ac.uk).

Deadline: 24 April 2019.

Flipping the switch; regulating protein synthesis in response to stress

Scientific background

All living organisms have adopted ways to maintain internal equilibrium and respond to stress factors. Consequently, they have evolved tightly regulated signalling pathways, which can sense changes in the environment and elicit a response.

In plants, like in most eukaryotes, the p70 ribosomal S6 kinases (S6Ks) pathway coordinates cell growth, cell proliferation, and stress response. Studies in Arabidopsis thaliana (Arabidopsis) have shown that, similarly to in humans, the S6K family is composed of two members, called AtS6K1 and AtS6K2, which function differently.

Little is known about AtS6K1 specific roles, despite initial evidences suggesting that it regulates responses to environmental stresses and developmental cues. The aim of this project is to unravel how AtS6K1 enables the plant to adapt to changes in the environment.

Research methodology

The successful candidate will carry out a structural characterisation of AtS6K1, alone and in complex with different substrates. Proteins structures will be solved using X-Ray crystallography. The atomic details obtained from the 3D structures will provide unique insights into how AtS6K1 is regulated, and will contextualise and rationalise in vivo and biophysical data, thus providing structure-function relationship. This project will set the base for future studies on the human kinase and on plant productivity.

Training

This project is highly interdisciplinary and the successful candidate will develop skills in recombinant protein expression, protein purification, protein extraction from leaves, structural biology (X-RAY, SAXS), and biochemical characterisation (SEC-MALS, fluorescence spectroscopy).

In addition to hands-on practical research skills, generic professional skills development will be supported internally via Proficio, the innovative professional development scheme available at University of Essex, or externally via Diamond Light Source, CCP4 and BAC training courses.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Filippo Prischi (fprischi@essex.ac.uk) and Dr Ulrike Bechtold (ubech@essex.ac.uk)

Closing date: 24 April 2019

High Throughput Drug Screening of a Cancer Target using Room Temperature Serial Crystallography

Microcrystals for serial crystallography have been successfully used to describe enzymatic reactions at ambient temperature. However, the possibility to use this novel and powerful technique to solve the structure of protein-ligand complexes has not yet been explored.

The aim is to solve the structure of a novel drug target, the heterogeneous nuclear ribonucleoprotein A1 protein (hnRNPA1), bound to different compounds using microcrystals for serial crystallography. hnRNPA1 holds great promise as a target for the treatment of Small Cell Lung Cancer (SCLC), an aggressive and fast spreading form of lung cancer with unmet clinical needs.

In fact, in SCLC activation of hnRNPA1 leads to downregulation of apoptosis and promotion of cell survival, resulting in resistance to chemotherapy. A such, compounds able to alter hnRNPA1 function could represent candidates for future drug development studies.

The studentship will work towards meeting the following objectives:

  • Recombinant protein production and crystallisation (months 1-3)
  • Measurement of serial crystallography (months 3-8)
  • Data analysis and structure interpretation (month 8-12)

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Mike Hough (mahough@essex.ac.uk) and Dr Filippo Prischi (fprischi@essex.ac.uk)

Closing date: 24 April 2019.

Molecular assembly and function of human Androglobin, an unusually large chimeric hemoglobin

Androglobin is a novel hemoglobin, discovered in 20121. The hemoglobin of the erythrocyte is one the most studied proteins in science, however androglobin is paradoxically one of the least studied and understood proteins of the hemoglobin superfamily.

The project aim is to investigate the structural and functional aspects of the heme domain of androglobin and its interaction with other androglobin domains or external proteins such as calmodulin through various biochemical experiments designed through the molecular modelling.

Conditions to generate crystal structures of the globin domain have so far eluded us, but the significant increase in spectra quality of the heme domain in the presence of calmodulin suggests that crystallizing the heme in the presence of other domains is likely to be successful.

Additionally, the protein will be expressed in human cancer cell lines, either transiently or through stably transfected protein, for cell stress studies. The unusual structural arrangement of this novel androglobin protein and the presence of calpain, known to control key physiological processes, make this a stimulating project with implications in male fertility issue and potentially cancer research.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Brandon Reeder (reedb@essex.ac.uk) and Professor Christine Raines (reync@essex.ac.uk)

Closing date: 24 April 2019.

Next generation SMALPs for purification of fully functional GPCRs 

The aim of this project will be to identify next generation (ng) SMALPs for functional extraction of G Protein-Coupled Receptors (GPCRs) from cell membranes. GPCRs are the largest family of plasma membrane proteins in humans and are targets of ~34% of approved drugs (annual global market $180 billion).

Current drug discovery platforms for GPCRs require structure/function approaches, often exploiting crystal and cryo EM structure models. However, extraction of GPCRS from cell membranes requires solubilization using detergents, agents that often destabilize the receptor causing it to unfold. 

The aims of this project are:

  1. To test ngSMA polymers designed to change the properties of SMALPs, including the numbers of lipids encapsulated.
  2. To examine the extent of extraction and the thermal stability of rhodopsin encapsulated in ngSMALPs.
  3. To examine the spectral and biochemical properties, including activation extent, of rhodopsin encapsulated in ngSMALPs

The MSD student will become a member of an international team investigating ngSMALPS with a focus on one of the most important classes of membrane receptors: GPCRs.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisor.

Supervisor: Dr Philip Reeves (preeves@essex.ac.uk)

Closing date: 24 April 2019.

Revealing the ancestral circadian clock

Circadian clocks are the underlying cause of jetlag, but they also play vital roles in metabolism and physiology in animals, plants, and bacteria. Despite being essential for correct cellular functions (the scientists who defined the molecular clock were awarded the Nobel prize in 2017), we do not understand the nature of the ancestral circadian system. Intriguingly, although ubiquitous in nature there is limited conservation of circadian clock components between kingdoms, demonstrating that these aspects of the circadian system have evolved independently in different lineages. As a consequence we still do not understand how the ancestral clockwork functioned, nor whether these functions have been retained.

The aims of this projects are:

  1. Purify and crystallise Arabidopsis thaliana JMJD5 (AtJMJD5). Construct will be designed based on the structure of human JMJD5.
  2. Confirm AtJMJD5 substrate, using recombinant GST-tag AtJMJD5 against candidate peptides.
  3. Examine the circadian pattern of ribosomal subunit phosphorylation in jmjd5 plants using existing antibodies.

Highly motivated applicants with, or expecting, a good degree in the broad area of Life Sciences are encouraged to apply.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisor.

Supervisors: Dr Matthew Jones (matthew.jones@essex.ac.uk) and Dr Filippo Prischi (fprischi@essex.ac.uk)

Closing date: 24 April 2019

Development of novel cancer treatments: structural studies of Nectin 4 in complex with bespoke anti-cancer peptides

This project targets the current gap in therapeutic approaches targeting Triple Negative Breast Cancer (TNBC) that, unlike other breast cancer subtypes, lacks recommended chemotherapy treatment. Recent studies suggest that Nectin-4 is a promising target for the treatment of TNBC.

Nectin-4 is expressed during foetal development, with expression declining in adult life, and it is re-expressed as a tumour-associated antigen with pro-oncogenic properties in TNBC and other cancers, including Bladder Cancer and Lung Cancer. Thus, Nectin-4 is both a promising new prognostic biomarker and specific therapeutic target for the treatment of TNBC.

Studies on patient samples show that Nectin-4 is highly expressed in cancer tissues, but is not detectable in healthy ones. The hypothesis is that targeting Nectin-4 with a peptide conjugated with toxin could provide a novel treatment for TNBC.

Novel compounds designed at our collaborators – Bicycle Therapeutics - are targeting Nectin-4 specifically at nanomolar range and can potentially be used as homing devices, having shown success in in vitro cell assays. However their mechanism of action and exact domain tropism is unknown.

In collaboration with Bicycle Therapeutics, we aim to solve the crystal structure of the extracellular domain of Nectin-4 bound to these proprietary cyclic peptides, which will guide further optimisation of the peptide before preclinical and clinical studies.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisor.

Supervisors: Dr Filippo Prischi (fprischi@essex.ac.uk) and Dr Vassily Bavro (v.bavro@essex.ac.uk)

Closing date: 24 April 2019

PhD studentships

PhD studentships are offered by the Faculty of Science and Health, the School of Biological Sciences, ARIES (NERC-funded Doctoral Training Partnership) and the EU (Horizon 2020). Details of our current opportunities are listed below. For further information, please contact the Graduate Administrator, Emma Revill (ecrix@essex.ac.uk).

Current PhD studentships

Departmental PhD studentship: Time-resolved synchrotron and XFEL crystallography of metalloenzymes using anaerobic photocages

X-ray crystallography has been the leading method to understand the structure and function of proteins and enzymes for decades. Despite this, it has a key limitation in that structures are not time-resolved and so do not represent the dynamic and changing nature of a protein’s structure as it carries out its function or enzymatic reaction. Time-resolved crystallography is one approach for capturing structures of reaction intermediates, though for probing fast changes approaches are typically limited to light activated processes.

Metalloproteins are vital to a wide range of biological functions and are particularly susceptible to site-specific radiation damage, a problem that is considerably worse when working at room temperature. Serial sample delivery and the use of photocages to trap and trigger reactions offer a means of resolving both of the above challenges, making fast time-resolved experiments applicable to a wide range of targets.

In this joint studentship between the University of Essex and Diamond Light Source you will perform cutting-edge research in the areas of metalloprotein structure determination, serial synchrotron crystallography (SSX), and X-ray free electron laser (XFEL) data collection to develop approaches for time-resolved SSX at Diamond. To this end you will exploit state-of-the-art fixed target instrumentation at Diamond and characterise photocages and their activation in crystals. Experiments and developments will be carried out using metalloproteins prepared by you at the University of Essex. There will also be the opportunity to carry out experimental work at the SACLA XFEL in Japan.

You will spend approximately half of the studentship based at the University of Essex and half based at Diamond.

Applications should be submitted electronically through our portal by the deadline, stating the title and supervisors.

Supervisors: Dr Mike Hough (mahough@essex.ac.uk) and Dr Robin Owen (robin.owen@diamond.ac.uk

Deadline: 8 April 2019

Faculty PhD studentship: Computational design of DNAzymes

You will gain skills in bioinformatics, statistics, machine-learning and drug design, alongside broader transferable research skills; producing a highly employable postdoctoral researcher, with a range of multidisciplinary skills.

Lead department: School of Biological Sciences (in collaboration with the School of Computer Science and Electronic Engineering)


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Faculty PhD studentship: Epigenetic machine learning: utilizing DNA methylation patterns to predict age acceleration

We are looking for a highly motivated and interdisciplinary minded student, who has an excellent computer science, bioinformatics, electronics or related UG/MSc degree and is keen to work on relevant research in the area of design deep learning architectures and algorithms for age prediction based on DNA methylation data.

Lead department: School of Computer Science and Electronic Engineering (in collaboration with the School of Biological Sciences)


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Faculty PhD studentship: Automated monitoring of animal health and welfare

This collaborative project brings together experts in mathematical modelling, data analysis and animal behaviour and welfare.

Lead department: Department of Mathematical Sciences (in collaboration with the School of Biological Sciences)


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PhD studentships - ARIES Doctoral Training Partnership

The ARIES (“Advanced Research and Innovation in the Environmental Sciences”) DTP trains postgraduate research students (PGRs) with excellent potential from across society, equipping them with the necessary skills to become 21st Century Scientists: leaders in the science and sustainable business of the natural environment. ARIES brings together expertise from five universities and over forty research-users.

We do not currently have any ARIES studentships available. If you would like more information about the ARIES DTP at Essex please email ariesapp@essex.ac.uk

Why should you do your research at Essex?

At the University of Essex, you can perform exciting research with excellent supervision that strikes the balance between guidance and encouraging independence.

You belong to intellectually stimulating research groups, and, importantly, will find a friendly, supportive environment within departments and across the university.

Through our unique professional development scheme Proficio, Essex provides outstanding financial support for training, field work, and conference participation.

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