FordLab


Professor Robert Ford's Website

Manchester Interdisciplinary Biocentre, Manchester, England

Guelph University, Canada



Current and Past Research of the Ford laboratory:

Our research interests centre on the understanding of the structure of membrane proteins. Earlier we focused on a group of membrane proteins that carry out the conversion of solar energy into chemical energy in photosynthetic organisms such as plants and algae. For example, we published the first glimpse of the 3D structure of photosystem I , (pub. 19), and in 1993, we published the first 3D structure of photosystem II. (pub. 23); these two represent amazingly complicated assemblages of proteins, pigments (such as chlorophyll) and electron transfer molecules. For photosystem II, and photosystem I we followed the systems biology strategy, and aimed to study the assembled proteins in a state as close as possible to their native one (pub. 35,39,48). Photosynthetic proteins are present in large amounts in solar energy-converting organisms, such as plants, so it is possible to purify them and study them relatively easily.

In the last 10-15 years there has been great progress in the production and purification of other membrane proteins (progress has been possible because of genetic engineering of membrane proteins). Hence over the past 10 years it has been possible to extend our research interests to a wider range of membrane proteins. We are particularly interested in a family of proteins that are involved in membrane transport (ABC transporters). The first insight into the 3D structure of this type of transporter emerged from our laboratory (pub. 31). We also produced the first crystals of these proteins (pubs. 43,45,53,56,63,65), opening up a route for the elucidation of their structure at using a method called electron crystallography. The latest 3D structure of P-glycoprotein at 8Å resolution has allowed us to identify its alpha-helical transmembrane segments (pub 77). Recently we have also obtained the first structural data for the complete CFTR protein, mutations of which are responsible for cystic fibrosis in humans (pub. 63). These various projects involve several biophysical approaches and much computational input. The projects are done in small groups because of the intensive training for the specialised technical skills that are required. list-of-publications