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Structural Biology

In the structural biology theme, X-ray crystallography and NMR are combined as extremely powerful techniques to explore the structure of macromolecules at the highest level of atomic detail. The dynamic behaviour of proteins in solution and how they assemble into their complex folds is explored, with emphasis on protein mis-folding in disease states such as Alzheimer's. High power electron and atomic force microscopy is used to visualise biological assemblies and processes directly, while complementary fluorescence microcopy is used to visualise complex organisation and localisation in vivo. Such large datasets require expertise in computational biology to analyse and interpret results.

Structural biology research in our department at a glance:

  • X-ray protein crystallographyprotein complexes, especially of toxins and virulence factors, protein/DNA interactions, drug design
  • Nuclear magnetic resonance spectroscopy (NMR)protein structure and dynamics, molecular interactions, ligand binding, high-pressure NMR
  • Complex imaging - fluorescence microscopy, electron microscopy (EM), atomic force microscopy (AFM), cryoelectron tomography
  • Computational biology - protein structure modelling, dynamic system modelling, image analysis

People

For further information and research opportunities, please see the staff page of individual researchers below:

bakerpDr Patrick Baker

Director of Studies
Deputy Head of Department

Room: D5d
Tel: 0114 222 2725
Email: p.baker@sheffield.ac.uk

Use of protein crystallography to study the structure/function relationships in biological macromolecules, including substrate specificity and chiral synthesis in enzymes and the molecular basis of stability in proteins from extremophiles.

Julien BergeronDr Julien Bergeron

Lecturer

Room: E36a
Tel: 0114 222 2854
Email: j.bergeron@sheffield.ac.uk

Using cryo-EM and other biophysical methods to study protein nano-machines, in particular the bacterial flagellum and the bacterial cytoskeleton.

bulloughpProfessor Per Bullough

Professor of Structural Biology

Room: E36e
Tel: 0114 222 4245
Email: p.bullough@sheffield.ac.uk

Solving the assembly and structure of large and challenging protein assemblies by high resolution electron microscopy (cryoEM) and X-ray crystallography, in particular bacterial endospores, cell surfaces and membrane protein complexes.

cravenjDr Jeremy Craven

Senior Lecturer

Room: D14b
Tel: 0114 222 4323
Email: c.j.craven@sheffield.ac.uk

Computational methods to model system dynamics in organisms, including hyphal tip growth in the pathogenic fungus Candida albicans, and peroxisome development in yeast. Image analysis.

hoiczykeDr Egbert Hoiczyk

Senior Lecturer

Room: F21
Tel: 0114 222 2733
Email: e.hoiczyk@sheffield.ac.uk

Using light and electron microscopy to study the structure and function of bacterial ultra-structure. Particular interest in bacterial cytoskeletons, gliding motility complexes and nano-organelles.

SelfPhD

hunternProfessor Neil Hunter FRS

Krebs Chair in Biochemistry

Room: E14a
Tel: 0114 222 4191
Email: c.n.hunter@sheffield.ac.uk

Biogenesis, structure, function and nanotechnology of photosynthetic membrane proteins from phototrophic bacteria and plants. Enzymology of the chlorophyll and carotenoid biosynthesis pathways.

hwanglDr Ling Chin Hwang

Lecturer

Room: F09a
Tel: 0114 222 2847
Email: l.hwang@sheffield.ac.uk

Multidisciplinary techniques such as single-molecule imaging, synthetic biology, biochemistry and microfluidics to study the molecular mechanisms of spatial organization in bacteria, such as cell division and chromosome segregation.

johnsonmDr Matt Johnson

Lecturer

Room: E6a
Tel: 0114 222 4418
Email: matt.johnson@sheffield.ac.uk

Photosynthetic dynamics; covering key apsects of thylakoid membrane organisation, membrane protein structure, light harvesting and electron transfer regulation and biommimetic photosynthetic systems.

raffertyjDr John Rafferty

Reader in Structural Biology

Room: D8a
Tel: 0114 222 2809
Email: j.rafferty@sheffield.ac.uk

Structural study of proteins and DNA primarily by X-ray crystallography and electron microscopy to gain 3D insights of biological macromolecules and their assemblies. Structure and function relationships.

ricedProfessor David Rice

Harrison Chair in Structural Biology

Room: D8c
Tel: 0114 222 4242
Email: d.rice@sheffield.ac.uk

X-ray crystallography in the analysis of enzyme structure and function to develop an understanding of basic biological mechanisms for rational design of new drugs and the use of enzymes for industrial and biomedical applications.

staniforthrDr Rosie Staniforth

Lecturer

Room: D7a
Tel: 0114 222 2761
Email: r.a.staniforth@sheffield.ac.uk

Structural and mechanistic studies on the mechanism of amyloid fibril formation, the precursor to neurodegenrative conditions including Alzheimer's disease.

SelfPhD

walthojProfessor Jon Waltho

Gibson Chair in Biophysics

Room: D12c
Tel: 0114 222 2717
Email: j.waltho@sheffield.ac.uk

Application of multidimensional NMR methods to solving protein structures, complex formation, kinetics, protein molecular recognition and transition states, particularly in kinases.

SelfPhD

williamsonmProfessor Mike Williamson

Head of Department

Room: D6a
Tel: 0114 222 4224
Email: hod.mbb@sheffield.ac.uk / m.williamson@sheffield.ac.uk

Protein structure determination, protein mobility and interactions with ligands by 2D and 3D NMR. Targets include bacterial pathogenesis proteins and human disease-state proteins.

SelfPhD