Department of Biochemistry University of Oxford Department of Biochemistry
University of Oxford
South Parks Road
Oxford OX1 3QU

Tel: +44 (0)1865 613200
Fax: +44 (0)1865 613201
Collage of Drosophila third instar larva optic lobe
Lu Yang, Davis lab
First year Biochemistry students at a practical class
Image showing the global movement of lipids in a model planar membrane
Matthieu Chavent, Sansom lab
Anaphase bridges in fission yeast cells
Whitby lab
Lactose permease represented using bending cylinders in Bendix software
Caroline Dahl, Sansom lab
Epithelial cells in C. elegans showing a seam cell that failed to undergo cytokinesis
Serena Ding, Woollard lab
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News

Cryo-EM sheds light on how cells repair DNA damage
Cryo-EM structure of human FANCD2/FANCI complex A new study has revealed the sequence of key events in an important DNA damage pathway. The work on the Fanconi anemia (FA) DNA repair pathway, from the labs of Dr. Martin Cohn in the department and Dr. Catherine Vénien-Bryan at the Pierre and Marie Curie University in Paris, has been published in Nature Communications Published: 13 July 2016
Dr Tim Nott awarded Wellcome Trust Sir Henry Dale Fellowship
Dr Tim Nott Dr Tim Nott has been awarded the prestigious Sir Henry Dale Fellowship from the Wellcome Trust, for his research into the emerging area of membraneless organelles Published: 16 June 2016
Matthieu Chavent receives PRACEdays16 Award
PRACEdays16 Dr. Matthieu Chavent recently received the PRACEdays16 Award for Best Scientific Presentation for his talk entitled "Membrane Protein Crowding: filling the gap between computations and experiments" Published: 19 May 2016

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Athena Swan Bronze Award

Vacancies

There are six job vacancies available

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Welcome

Mark Sansom, Head of Department

Welcome to the Department of Biochemistry, part of the University of Oxford's Medical Sciences Division. We are one of the largest Biochemistry departments in the world and carry out world-class research and teaching. Our researchers come from a range of disciplines and work in a collaborative environment on all aspects of modern molecular and cellular biochemistry. We hope you enjoy reading more about our activities on these pages.

Professor Mark Sansom, Head of Department

News Highlight

Protein sensor turns itself inside out and back again

New research has uncovered the molecular details of how bacteria deal with oxidative stress.

Colin Kleanthous in the department, in collaboration with Jennifer Potts at the University of York and colleagues in Oxford, has published the work in Nature Communications (1). By elucidating the structure and dynamic behaviour of a key protein in a stress-response pathway, they have revealed a new way in which stress sensors in general may function.

Streptomyces colonies

Streptomyces colonies. Credit: Mark Buttner, John Innes Centre

All bacteria have sigma factors, proteins that initiate transcription by binding to RNA polymerase. Sigma factors can regulate how bacteria respond to extracellular stresses, which can be diverse – from nutritional cues, to changes in oxidative state or temperature. For some sigma factors, the regulation is imposed by a group of proteins called zinc-binding anti-sigma factors (ZAS). In this system, the ZAS protein rather than the sigma factor responds to stress. ZAS protein and sigma factor are bound in a tight complex in the resting state. When a cue is received, the ZAS protein releases the sigma factor, enabling it to switch on genes that will neutralize the stress.

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Seminars

Biochemistry Department Seminar Dr. Dirk Schübeler, 'Title TBC' Monday 17th Oct, 13:00 Main Seminar Room, New Biochemistry Building
Biochemistry Department Seminar Professor Sadaf Farooqi PhD, FRCP, FMedSci, 'Title TBC' Monday 5th Dec, 13:00 Main Seminar Room, New Biochemistry Building
Biochemistry Department Seminar Professor Jernej Ule, 'Title TBC' Monday 9th Jan, 13:00 Main Seminar Room, New Biochemistry Building
Biochemistry Department Seminar Professor A.P. Waters, 'Title TBC' Monday 16th Jan, 13:00 Main Seminar Room, New Biochemistry Building


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