Welcome
The Department of Biochemistry at the University of Oxford is a centre for world class research and teaching of all aspects of Biochemistry by staff from many different backgrounds and nationalities. Our research addresses a wide range of questions relating to the fundamental basis of all cellular life from man to microbes. This work explains the structures and functions of proteins and nucleic acids, and in doing so addresses the mechanisms of many human diseases. Using this knowledge, other researchers aim to create new vaccines, antiviral and antibacterial therapies to protect and treat humans across the world.
You can read more about the details of our current work and other aspects of the department, including undergraduate teaching and public outreach activities, on these web pages.
Professor Mark Sansom, Head of Department
News Highlight
Water-bridging as an essential component for initiating protein folding
The mechanism by which proteins fold from their primary sequence, encoded by DNA, into their specific three dimensional functional structure is still not understood. In nature, this process occurs spontaneously, and relatively quickly, and in water. While there must be an interplay between the specific sequence of the protein and the surrounding water solvent for folding to occur in nature, there is still an ongoing debate concerning how water molecules aid in driving folding. One difficulties in investigating the role of water in this process is because naturally occurring proteins fold rapidly and as a result, it is difficult to observe proteins in the process of folding, especially in the initial stages, by many experimental techniques.
Figure 1 showing the water bridge in KGPGK
A recent publication in the Journal of the American Chemical Society from research performed in the McLain Group from DPhil student Nicola Steinke, has focused on investigating the roles that both water and the primary amino acid sequence have in initiating β-turn formation in solution. By using a combination of techniques which provide information at the atomic level - neutron and X-ray diffraction and computer simulations - the interplay between conformation and hydration for five KGXGK peptides (with X=P,G,S or L) in the process of folding has been determined.
