Proteins are large molecules, made up of strings or ‘sequences’ of amino acids that twist and fold into complex three-dimensional shapes.
These shapes determine how they bind to other molecules in our bodies, affecting a whole host of vital biological functions such as immune responses or the development of genetic diseases.
Determining the shapes of proteins has been a long-standing problem in science. Today, scientists have determined over 150 million protein sequences but only under 100,000 different structures.
Phyre, developed by Professor Michael Sternberg’s group, is an internationally-used software suite that predicts three-dimensional protein structures from sequences. Since 2013, it has over 500,000 distinct users from over 80 countries, including over 900 commercial users.
Phyre uses the most accurate approach of determining protein structure by modelling an unknown shape based on the known structure of an evolutionarily-related protein, known as the template. Combining this powerful algorithm with extensive web-based functionality, users all over the world are able to use Phyre in pharmaceuticals, biotechnology and agritechnology.
Professor Sternberg’s software has impacted science’s understanding of genetic mutations associated with disease, vaccine design and therapeutic antibodies.
Postgraduate research
Interested in studying a PhD at the Department of Life Sciences? Find out more about postgraduate research opportunties.