Abstract
BiopolymersVolume 109, Issue 7 e23055 ISSUE INFORMATIONFree Access Issue Information First published: 14 August 2018 https://doi.org/10.1002/bip.23055AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Graphical Abstract Collagen fibrils are the major component of the molecular scaffold of connective tissues such as bones, skin and blood vessel walls. Strawn et al. report a novel protein design strategy to create collagen-like fibrils having the characteristic axial repeating structure known as the D-period. Specific periodic placement of selected amino acids gives rise to collagen-like fibrils emerging as the unique, most stable conformation during the self-association of collagen triple helices. Achieving the structural features of collagen fibrils suggests a way forward to produce bottom-up, designed collagen-based biomaterials for a wide range of applications. (DOI: 10.1002/bip.23226) Volume109, Issue7July 2018e23055 RelatedInformation
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