ISIS Neutron and Muon Source Data Journal

Elucidating the unique role of non-standard collagen helices in forming key protein-protein complexes

Abstract: 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.

Principal Investigator: Professor Stephen Perkins
Experimenter: Miss Hina Iqbal
Local Contact: Dr James Doutch

DOI: 10.5286/ISIS.E.RB1810746

ISIS Experiment Number: RB1810746

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Professor Stephen Perkins et al; (2018): Elucidating the unique role of non-standard collagen helices in forming key protein-protein complexes, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1810746

Data is released under the CC-BY-4.0 license.