Summer Research Lab Experience 2016


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 2016 at the latest or by the date specified for specific projects below. When contacting supervisors please forward a copy of your current CV and a brief statement outlining your interest in the project and your suitability.

Projects available for Summer 2016

Studying protein folding on the ribosome during biosynthesis using NMR spectroscopy and MD simulations

Within every cell, polypeptides chains emerge from the ribosome during biosynthesis, and can either fold successfully to form their 3D structure, however under some circumstances, can also readily misfold, leading in some cases to the formation of toxic, disease-causing aggregates. In our laboratory, we are interested in understanding the very earliest events that newly synthesized polypeptide chains encounter, and by using a combination of techniques: NMR spectroscopy, molecular dynamics simulations and biochemical techniques, we study how protein structure is formed during translation on the ribosome (see Figure). In our recent structural studies of translationally-arrested ribosome-nascent chain complexes (RNC), we have produced the first 3D structural ensemble model of an emerging nascent chain, and show how the ribosomal surface is implicated in modulating the process of protein folding. Using protein engineering and gene-editing strategies, we are currently exploring a molecular level details of co-translational folding, as well as the reasons that drive proteins towards aberrant folding processes that ultimately lead to disease.



Figure:(a) 1H-13C spectra of FLN5 with selective labeling of its isoleucine residues: isolated FLN5 protein (top) and as a ribosome-nascent chain complex (bottom).

(b) NMR chemical shifts are used as restraints within MD simulations to generate 3D ensemble structures of the FLN nascent chain when it is bound to the ribosome. (Inset) The folding of the FLN nascent chain is influenced by the contacts that it makes with ribosomal RNA and proteins.


Building a computational pipeline for microtubule structure determination

Microtubules are centrally involved in many facets of cell biology. Studying microtubules and their cellular regulators at the molecular level can thus shed light on fundamental mechanisms of control and how disruption of such control contributes to human disease. Cryo-electron microscopy (cryo-EM) provides unprecedented insight into the operation of the macromolecular machinery that drives cell life and is uniquely suited to the study of microtubules (1,2). Due to breakthroughs in imaging technology, cryo-EM is currently undergoing a revolution such that visualisation of near-atomic resolution structures is becoming more routine (2,3).

The aim of this interdisciplinary project is to help build a pipeline for cryo-EM data processing of microtubules and their binding partners to facilitate structure determination to near-atomic resolutions. Through scripting, data management and analysis of quality measures for sorting the large and noisy datasets, this project will enable robust semi-automation of processing procedures to allow an increase in data throughput. Streamlining of our image processing procedures will allow identification of bottlenecks and limitations in our current data handling schemes. This in turn, will enable us to modify or design new sample preparation or data collection strategies to further harness the power of this cutting-edge structural biology technique.


  1. Atherton et al (2014). Conserved mechanisms of microtubule-stimulated ADP release, ATP binding and force generation. Elife 3, e03680
  2. Zhang et al (2015). Mechanistic origin of microtubule dynamic instability and its modulation by EB proteins. Cell 162, 849-859
  3. Kuhlbrandt (2014). The resolution revolution. Science 343, 1443-1444

Project supervisor/ host lab
Professor Carolyn Moores and Dr Joseph Atherton ISMB, Birkbeck College

  • Contact
  • Requirements
    Applicants should be in their penultimate year of 1) a biochemistry degree and have a strong interest in computing) or 2) a computing degree and have a strong interest in biology and be eligible to apply for studentship funding.
  • Deadline for students to make contact
    5 January 2016

Interactions of complement factor H with its ligands

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.

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

  • Contact
  • Requirements
    Ideally taking BIOC2004 and/or IMMU2001. Please provide your PORTICO printout when applying.
  • Deadline for students to make contact
    15 January 2016. Please also provide a brief CV and the name of a referee.






Institute of Structural and Molecular Biology, University of London
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