Collagen is the most abundant protein in mammals and makes up about 30% of our body weight. Not so much of a surprise therefore, that molecular errors in collagen are implicated in many diseases, and that collagen is also a key biomaterial, for example as a matrix for growing cells in regenerative medicine. Collagen is also the prime natural example of hierarchical assembly in biology: collagen polypeptides assemble into triple helices, triple helices assemble into proto-filaments, proto-filaments assemble into fibrils, fibrils assemble into fibers, etc. We want to understand how this hierarchical self-assembly is encoded in the primary sequence of collagen proteins. Ideally we would like to understand it so well that we can design our own collagen molecules, that should self-assemble in a way designed by us, for example for use in regenerative medicine. Research in the protein materials group focusses on the step of the assembly of triple helices into staggered fibrils (see images). We work along two lines: computer simulations on simplified models of collagen triple helices, and protein engineering to design simple self-assembling collagens, based on sequences for primitive bacterial collagens that by themselves do not yet self-assemble.
Techniques (experimental): in-silico DNA design, molecular cloning, protein expression in E. coli, protein purification & characterisation (SDS-PAGE, mass spectrometry), protein spectroscopy (Circular Dichroism, Differential Scanning Calorimetry, Electron Microscopy, Atomic Force Microscopy
Techniques(theoretical): Langevin Dynamics computer simulations, Molecular Dynamics Computer Simulations, Python programming