The collagens are the most abundant proteins in mammalian systems, comprising up to 25% of human proteins. Their three-stranded triple helix structures are a major determinant of their function. Our work on basic triple helix structures by SAXS and atomistic modelling revealed previously unknown flexibility and bends in its linear structure. Our efforts to repeat this work for more specialized triple helices in the complement proteins were held up by severe X-ray radiation damage. Test neutron scattering gave excellent results. We will thus compare the structures of basic and specialized triple helical peptides using a combination of neutron and X-ray scattering, ultracentrifugation and advanced atomistic modelling in CCP-SAS. An understanding of these collagen structures will provide essential new insights for understanding the molecular properties of triple helices and their function.