Willie Taylor

Computational Cell and Molecular Biology Laboratory

Proteins are the main essential active agents in biology and without them, almost none of the processes that we associate with life would take place. Proteins enact their tasks, not as the linear sequence of amino acids that defies their uniqueness, but more typically as a compact three-dimensional structure. My group aims to try to understand the relationship between the protein sequence and its structure and hence the function.

Such studies can help us to understand the workings of normal proteins and also how abnormal states, such as mutant proteins, can lead to disease. Computer methods that we have developed have been used to construct models for all possible protein folds and we find that only 10 per cent of these model structures correspond to known folds. The remainder, which we call 'dark' folds, appear quite normal under all the computer tests we have applied. We are currently using some of these folds as frameworks for design and synthesis.


A view of protein fold space showing the location of 'dark' folds (white) between known fold families (red, green) with example structures marked by stars. (Click to view larger image)

Selected publications

Sadowski, MI and Taylor, WR (2010) Protein structures, folds and fold spaces. Journal of Physics-Condensed Matter 22, 033103

Macdonald, JT; Maksimiak, K; Sadowski, MI and Taylor, WR (2010) De novo backbone scaffolds for protein design. Proteins 78, 1131-1325

Taylor, WR; Chelliah, V; Hollup, SM; MacDonald, JT and Jonassen, I (2009) Probing the "dark matter" of protein fold space. Structure 17, 1244-1252