World-class research
Structural Biology, Bioinformatics and Biophysics
Some research highlights
Investigators at the School of Crystallography at Birkbeck College are engaged in world-class research in many aspects of structural biology, computational biology, biophysics and materials science. Many of their achievements have led to greater understanding of biological processes that lead to human disease and have potential applications in drug design. The School has excellent in-house facilities for molecular biology, X-ray protein crystallography, electron microscopy, circular dichroism and a wide range of biophysics instrumentation.
Recently, researchers in the department have solved the structure of a protein in Mycobacterium tuberculosis that plays an important role in its infectivity; deciphered a small part of the puzzle of the DNA replication process; and demonstrated how proteins secreted by some types of bacteria can “punch holes†in cell membranes to kill the cells.
Streptococcus pneumoniae, as its name implies, is a bacterium that can cause pneumonia. Renowned electron microscopist Helen Saibil, with colleagues at Birkbeck and collaborators from Leicester and Oxford, showed for the first time how the protein pneumolysin, secreted by this micro-organism, could assemble into a ring-like structure on the surface of a human cell and bore itself through the cell membrane to form a pore, leading to lysis of the cell's contents and subsequently cell death. Pore formation is accompanied by a dramatic change in the conformation of the protein monomer. Professor Saibil was the last Ph.D. student of Nobel Prizewinning DNA pioneer Maurice Wilkins, who died in 2004.
Professor Gabriel Waksman joined Birkbeck and UCL in 2003 from Washington University School of Medicine in St. Louis. His group is studying protein-protein interactions using biophysical techniques including fluorescence resonance energy transfer (FRET) and calorimetry. They discovered that the enzyme DNA polymerase, which catalyses the addition of nucleotides to a growing DNA strand closes its grip on the growing strand extremely rapidly, but only forms a stable complex if the complex includes a complementary nucleotide.
These discoveries are described in more detail on the ISMB website, with links to the original publications.
In the field of bioinformatics, Professor David Moss and his colleagues are part of a consortium that was awarded almost 2 million euros by the European Commission in 2005 for a project to model the human immune system.
85% of our research was recognised as having international impact in RAE 2008, with 15% receiving the highest possible rating of world-leading.
© 2005 School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK
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