Small angle x-ray scattering is one of the most flexible and readily available experimental methods for obtaining information on the structure of proteins in solution. In the advent of powerful predictive methods such as the alphaFold and rossettaFold algorithms, this information has become increasingly in demand, owing to the need to characterise the more flexible and varying components of proteins which resist characterisation by these and more standard experimental techniques. To deal with structures about little of which is known a parsimonious method of representing the tertiary fold of a protein backbone as a discrete curve has been developed. It represents the fundamental local Ramachandran constraints through a pair of parameters and is able to generate millions of potentially realistic protein geometries in a short space of time. The data obtained from these methods provides a treasure trove of information on the potential range of topological structures available to proteins, which is much more constrained that that available to self-avoiding walks, but still far more complex than currently understood from existing data. I will introduce this method and its considerations then attempt to pose some questions I think topological data analysis might help answer. Along the way I will ask why roadies might also help give us some insight….
