Journal article

Sub-Angstrom structure of collagen model peptide (GPO)(10) shows a hydrated triple helix with pitch variation and two proline ring conformations

Hironori Suzuki, Deepti Mahapatra, Amanda J Board, Peter J Steel, Jolon M Dyer, Juliet A Gerrard, Renwick CJ Dobson, Celine Valery

Food Chemistry | ELSEVIER SCI LTD | Published : 2020


Collagens are large structural proteins that are prevalent in mammalian connective tissue. Peptides designed to include a glycine-proline-hydroxyproline (GPO) amino acid triad are biomimetic analogs of the collagen triple helix, a fold that is a hallmark of collagen-like sequences. To inform the rational engineering of collagen-like peptides and proteins for food systems, we report the crystal structure of the (GPO)10 peptide at 0.89-Å resolution, solved using direct methods. We determined that a single chain in the asymmetric unit forms a pseudo-hexagonal network of triple helices that have a pitch variation consistent with the model 7/2 helix (3.5 residues per turn). The proline rings occu..

View full abstract


Awarded by Ministry of Business, Innovation and Employment

Awarded by New Zealand Royal Society Marsden Fund

Awarded by U.S. Army Research Office

Funding Acknowledgements

HS acknowledges the Royal Society of New Zealand and the Japan Society for the Promotion of Science for salary support by the FY 2012 Researcher Exchange Program. RCJD acknowledges the following for funding support, in part: 1) the Ministry of Business, Innovation and Employment (contract UOCX1208); 2) the New Zealand Royal Society Marsden Fund (contract UOC1013); and 3) the U.S. Army Research Laboratory and U.S. Army Research Office (contract/grant number W911NF-11-1-0481). We thank Jackie Healy for her support in managing the lab involved in this project work.