The supramolecular structure of bone: X-ray scattering analysis and lateral structure modeling.

ABSTRACT: The evolution of vertebrates required a key development in supramolecular evolution: internally mineralized collagen fibrils. In bone, collagen molecules and mineral crystals form a nanocomposite material comparable to cast iron in tensile strength, but several times lighter and more flexible. Current understanding of the internal nanoscale structure of collagen fibrils, derived from studies of rat tail tendon (RTT), does not explain how nucleation and growth of mineral crystals can occur inside a collagen fibril. Experimental obstacles encountered in studying bone have prevented a solution to this problem for several decades. This report presents a lateral packing model for collagen molecules in bone fibrils, based on the unprecedented observation of multiple resolved equatorial reflectio

SUBMITTER: Zhou HW 

PROVIDER: S-EPMC5013594 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature