Summer Research Lab Experience 2018


Join one of our research teams

You will be a member of one of our research teams, and your work will be an important contribution to the group’s discoveries. Summer research lab experience is an invaluable opportunity to gain hands-on experience in a research group and to get career advice from fellow students and mentors. They are also a great way to meet new people; we are a small, friendly department, located in the heart of London.


Opportunities are largely funded by the Wellcome Trust or other learned societies. In order to be eligible for a research bursary from these organisations you must be:

  • Taking an undergraduate science degree
  • Considering research as a career
  • Expecting to achieve a First Class or good Upper Second Class degree result (references will be required)
  • In the middle years of your degree e.g. your visit will take place in the Summer vacation before the start of the final year of study
  • Registered at a UK university for the majority of your degree (for most funding bodies)

Working hours and stipend

  • Working hours will be 35 hours per week for between 6-8 weeks.
  • You can expect to receive a stipend of between £180 and 200 per week during your stay if the application for funding is successful. There are also opportunities for unpaid research lab experience.

How to apply

  • Potential applicants should contact chosen project supervisors by the end of January 2017 at the latest or by the date specified for specific projects below.
  • When contacting supervisors please forward: a copy of your current CV; a brief statement of support outlining your interest in the project and your suitability; the name of an academic referee.

Projects available for Summer 2018


Molecular Mechanisms of Drug Efflux and Biofilm in Antibiotic Resistance

Project supervisor/ host lab
Dr Sanjib Bhakta, Department of Biological Sciences, UCL

The rise of antimicrobial resistance is leading to ever-more untreatable illness. Intracellularly surviving bacterial pathogens have endogenous machinery to evade host defence as well as antibiotic treatment. Drug efflux and formation of biofilms are the two key fundamental mechanisms of intrinsic resistance which renders many antibiotics ineffective against them. Bacteria have unique multi-drug transporter protein complexes that allow the pathogen to take up nutrients for survival while allowing it to extrude deleterious ones so as the signalling molecules for quorum-sensing leading to biofilm formation. Aim of this project is to characterise the molecular mechanisms to inform new drug-discovery as well as repurposing existing drugs with the aim of reversing antimicrobial resistance. This interdisciplinary research project will offer the candidate training in molecular biology, biochemistry and microbiology research, providing experience of drug discovery.



  1. Repurposing drugs for treatment of tuberculosis: a role for non-steroidal anti-inflammatory drugs. (2016) Maitra A, Bates S, Shaik M, Evangelopoulos D, Abubakar I, McHugh TD, Lipman M, Bhakta S. Br Med Bull. 118(1):138-48. doi: 10.1093/bmb/ldw019.
  2. Repurposing-a ray of hope in tackling extensively drug resistance in tuberculosis. (2015) Maitra A, Bates S, Kolvekar T, Devarajan PV, Guzman JD, Bhakta S. Int J Infect Dis. 32:50-5. doi: 10.1016/j.ijid.2014.12.031.
  3. Antitubercular specific activity of ibuprofen and the other 2-arylpropanoic acids using the HT-SPOTi whole-cell phenotypic assay. (2013) Guzman JD, Evangelopoulos D, Gupta A, Birchall K, Mwaigwisya S, Saxty B, McHugh TD, Gibbons S, Malkinson J, Bhakta S. BMJ Open. 20;3(6). pii: e002672. doi: 10.1136/bmjopen-2013-002672.
  4. Nonsteroidal anti-inflammatory drug sensitizes Mycobacterium tuberculosis to endogenous and exogenous antimicrobials. (2012) Gold B, Pingle M, Brickner SJ, Shah N, Roberts J, Rundell M, Bracken WC, Warrier T, Somersan S, Venugopal A, Darby C, Jiang X, Warren JD, Fernandez J, Ouerfelli O, Nuermberger EL, Cunningham-Bussel A, Rath P, Chidawanyika T, Deng H, Realubit R, Glickman JF, Nathan CF. Proc Natl Acad Sci U S A. 2;109(40):16004-11. doi: 10.1073/pnas.1214188109.

Mechanisms of aggregation of the disease-associated protein α1-antitrypsin

Project supervisor/ host lab
Dr James Irving, Lomas Laboratory, UCL Respiratory, Rayne Building, UCL

α1-Antitrypsin is a plasma protein that protects the lungs from damage during an inflammatory response. Defects in this protein cause a type of disease called a serpinopathy - part of a broader class of protein conformational diseases that includes Alzheimer's and Huntington's - and is the subject of at least five current drug discovery programmes within the pharmaceutical industry. As a potential drug target, α1-antitrypsin presents unique challenges, because its pathogenicity is associated with a conformational change that results in formation of an ordered aggregate called a polymer. The most common pathological 'Z' mutation causes polymers to form insoluble deposits within liver cells, predisposing individuals to cirrhosis, as well as emphysema due to a protease-antiprotease imbalance in the lung.

The student will have the opportunity work in a multi-disciplinary laboratory that is using structural, biophysical, genetic, clinical and cell-based techniques to understand the molecular mechanisms of this class of disease. Because structural change is fundamental to the physiological role as well as pathology of α1-antitrypsin, we have produced conformation-specific monoclonal antibodies to monitor its behaviour. These antibodies are being used as probes of changes that occur during polymerisation. This project will involve the use of electron paramagnetic resonance spectroscopy, FRET, custom conformation-specific monoclonal antibodies, protein expression and purification, and protein functional characterisation to undertake fundamental research in order to contribute to an important clinical aim.

Anticipated outcomes: (1) Experience in recombinant protein expression, purification and characterisation; (2) use of biophysical approaches to identify the site of protein-protein interactions and identify structural consequences of defects in protein stability; (3) the use of chemical probes and antibody-based techniques to track structural changes that occur during polymerisation; and (4) an evaluation of the data against structural models to draw conclusions regarding the mechanism of polymerisation.


Summer internships in Bioinformatics lab of Dr Irilenia Nobeli

Project supervisor/ host lab
Dr Irilenia Nobeli, Department of Biological Sciences, Birkbeck

Summer internships in the bioinformatics lab of Dr Nobeli will be available in one of the three areas of research focus in the group:

a) The development and application of computational methods for quantifying the differential use of alternative transcription start site and alternative poly-adenylation of eukayryotic transcripts and the effects that shortening or lengthening the ends of a gene might have on the fate and function of that gene.
b) The analysis of transcriptomic (NGS) data relating to neurodevelopmental diseases (in particular autism).
c) The structural and phylogenetic analysis of riboregulators in bacteria.

A project will be designed to fit the student's skills and interests.

The ideal applicant will be competent in using computers (preferably have experience with Unix-based OS) and will have some basic training in R and statistics. Experience in programming in any language would be an advantage.

Students looking for funding should identify a funding body and apply to the group at least 4 weeks ahead of the deadline for funding applications.


Interactions of complement factor H with its ligands

Project supervisor/ host lab
Prof Steve Perkins, Molecular Interactions Facility, Structural Immunology Group, UCL.

Ideally taking BIOC2004 and/or IMMU2001 (or equivalent if not a UCL student). Students should provide a transcript of their results when applying.

Age-related macular degeneration (AMD) is the main cause of blindness in the Western World in people over 55 years. Deposition of proteins, ions and lipids as "drusen" between the blood circulation and the retina is a major risk factor in AMD. Drusen usually grow in size and spread with age, disrupting the normal function of the retina, but may disappear. We recently discovered that the interaction between C-reactive protein and complement factor H may be a crucial factor in AMD (“Paper of the Week” in J.Biol.Chem. in January 2010). In order to prove further the involvement of intact complement factor H with this (or other ligands), the summer project will involve the purification of the homozygous high-risk and low-risk forms of factor H from patient plasma, then measurements will be made using surface plasmon resonance to define the conditions under which Factor H will interact with C-reactive protein (or other ligands) on sensor surfaces to which Factor H or C-reactive protein has been immobilised.

Deadline for students to make contact: about 15th January 2018.


Building the cilium with ATP-driven molecular motors

Project supervisor/ host lab
Dr Anthony Roberts, ISMB

Virtually every cell type in the human body builds a cilium: a microtubule-based projection from the plasma membrane. It has emerged that these antennae-like structures are crucial for sensing light, smell, fluid flow, and morphogens. Their dysfunction is associated with obesity, kidney disease, and developmental defects. 
How the cell builds the cilium – a complex organelle with defined size, architecture, and protein composition – is a major unsolved question. Central to cilium construction are the molecular motors kinesin and dynein. These motor proteins transport building blocks and signaling molecules to and from the cilium tip, using ATP hydrolysis to move along ciliary microtubules. 
Elucidating the structure and mechanism of the ciliary motor protein complexes has been challenging, in part because they are formed by large subunits that fail to fold correctly when expressed in bacteria. The goal of this project is to use a newly developed insect cell expression system [1] to produce and analyze protein constructs and thereby investigate how the motors move and are regulated. In addition to molecular biology and biochemistry, core techniques in the lab are electron microscopy and single-molecule fluorescence microscopy, which enables visualization of individual motor protein movements.


  1. [1] Toropova, K., Mladenov, M., and Roberts, A.J. (2017) Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements. Nature Structural & Molecular Biology 24, 461–468.

Exploring lipid membrane adhesion and signal amplification

Project supervisor/ host lab
Dr Salvador Tomas, Department of Biological Sciences, Birkbeck

Among other processes, cell communication often requires the membranes of two cells to come into close contact. At the molecular level, this event is facilitated by specialized membrane proteins that assemble laterally within each of the cells at the point of contact, and bind across to each other cell membrane. We have recently developed a model of membrane receptor lateral assembly, using non-biological (synthetic), model receptors, and lipid vesicles as model cell membranes. We hypothesise the lateral assembly of receptors within the membrane of a lipid membrane, and that of ligands within the membrane of a second lipid membrane can modulate the adhesion between the lipid vesicles, leading to an on/off signal amplification event following small environmental changes. The aim of this project is to synthesise a series of suitable membrane anchored ligands and to study their lateral assembly upon exposure to their receptors. This simple formulation will allow us to study these processes in a level of detail that cannot be attained within the molecular complexity of living cells. In the long term, these studies will enable the development of a mathematical model of membrane adhesion and the concurrent signal amplification. You will use the following techniques:

  • Chemical synthesis
  • HPLC to purify products of synthesis
  • NMR to characterise products of synthesis
  • Fluorescence and/or UV/Vis spectroscopy to characterise the ligand assembly within the lipid membrane.

Understanding how supernumerary subunits and allosteric factors can regulate cytochrome c oxidase core activity

Project supervisor/ host lab
Dr Amandine Marechal

Cytochrome c oxidase (CcO) is the terminal enzyme of our respiratory chains. It is a large membrane protein (200kDa) composed of 13 subunits. Three are encoded by the mitochondrial DNA and form the catalytic core but the function of the ten other subunits, which are nuclear DNA encoded and unique to mitochondrial forms of the enzyme, remains unknown. It has recently been proposed that they would have evolved in eukaryotes to control and regulate the activity of the mitochondrial encoded subunits, in a process comparable to a ‘domestication scenario’. This is a rather poorly studied area and little is known about the actual mechanism of such processes.

This project will focus on understanding the mechanism of the reported inhibition of CcO by ATP. We will use the yeast CcO as a model system of the human enzyme to characterise the site where ATP interacts/binds to the protein through activity assays ran on a range of supernumerary subunit mutants. We will then aim to unravel the details of the mechanism at the molecular level using specialist techniques such as FTIR spectroscopy.



Institute of Structural and Molecular Biology, University of London
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