title: Differential contributions of conformation extension and domain unfolding to properties of fibronectin nanotextiles.
abstract: Fibronectin (FN) textiles are built as nanometer-thick fabrics. When uniaxially loaded, these fabrics exhibit a distinct threshold between elastic and plastic deformation with increasing stretch. Fabric mechanics are modeled using an eight-chain network and two-state model, revealing that elastic properties of FN depend on conformational extension of the protein and that plastic deformation depends on domain unfolding. Our results suggest how the molecular architecture of a molecule can be exploited for designer mechanical properties of a bulk material.
authors.affiliation: Disease Biophysics Group, Wyss Institute for Biologically Inspired Engineering, Boston, Massachusetts 02115, USA.
authors.forename: Leila F
authors.initials: LF
authors.lastname: Deravi
authors.forename: Tianxiang
authors.initials: T
authors.lastname: Su
authors.forename: Jeffrey A
authors.initials: JA
authors.lastname: Paten
authors.forename: Jeffrey W
authors.initials: JW
authors.lastname: Ruberti
authors.forename: Katia
authors.initials: K
authors.lastname: Bertoldi
authors.forename: Kevin Kit
authors.initials: KK
authors.lastname: Parker
mesh_terms: D019281:Dimerization; D004548:Elasticity; D005109:Extracellular Matrix / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry*; D015233:Models, Statistical; D008968:Molecular Conformation; D055095:Optics and Photonics; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013784:Textiles
chemical_list: D005353:Fibronectins