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Extracting the 3D fibril structure from 2D small\u2010angle X\u2010ray scattering before and during physiological compression reveals of dominant deformation modes, including crystallinity transitions, lateral fibril compression, and reorientation, which vary in a coupled, nonlinear, and correlated manner across the cartilage\u2010bone interface. A distinct intermolecular arrangement of collagen molecules, and enhanced molecular\u2010level disorder, is found in the cartilage (sliding) surface region. Just below, fibrils accommodate tissue strain by reorientation, which transitions molecular\u2010level kinking or loss of crystallinity in the deep zone. Crystalline fibrils laterally shrink far more (20\u00d7) than they contract, possibly by water loss from between tropocollagen molecules. With the calcified plate acting as an anchor for surrounding tissue, a qualitative switch occurs in fibrillar deformation between the articular cartilage and calcified regions. These findings significantly advance this understanding of the complex, nonlinear ultrastructural dynamics at this critical interface, and opens avenues for developing targeted diagnostic and therapeutic strategies for musculoskeletal disorders.<\/jats:p>","DOI":"10.1002\/advs.202407649","type":"journal-article","created":{"date-parts":[[2024,11,11]],"date-time":"2024-11-11T14:05:11Z","timestamp":1731333911000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Nonlinear Stress\u2010Induced Transformations in Collagen Fibrillar Organization, Disorder and Strain Mechanisms in the Bone\u2010Cartilage Unit"],"prefix":"10.1002","volume":"12","author":[{"given":"Waqas","family":"Badar","sequence":"first","affiliation":[{"name":"Centre for Bioengineering and School of Engineering and Materials Science Queen Mary University of London  London E1 4NS UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sheetal 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