title: The effect of cross-link distributions in axially-ordered, cross-linked networks.
abstract: Cross-linking between the constituent chains of biopolymers has a marked effect on their materials' properties. In certain of these materials, such as fibrillar collagen, increases in cross-linking lead to an increase in the melting temperature. Fibrillar collagen is an axially-ordered network of cross-linked polymer chains exhibiting a broadened denaturation transition, which has been explained in terms of the successive denaturation with temperature of multiple species. We model axially-ordered, cross-linked materials as stiff chains with distinct arrangements of cross-link-forming sites. Simulations suggest that systems composed of chains with identical arrangements of cross-link-forming sites exhibit critical behavior. In contrast, systems composed of non-identical chains undergo a crossover. This model suggests that the arrangement of cross-link-forming sites may contribute to the broadening of the denaturation transition in fibrillar collagen.
authors.affiliation: Department of Physics, University of South Florida, Tampa, FL 33620, USA.
authors.forename: C Brad
authors.initials: CB
authors.lastname: Bennett
authors.forename: James
authors.initials: J
authors.lastname: Kruczek
authors.forename: D A
authors.initials: DA
authors.lastname: Rabson
authors.forename: W Garrett
authors.initials: WG
authors.lastname: Matthews
authors.forename: Sagar A
authors.initials: SA
authors.lastname: Pandit
mesh_terms: D001665:Binding Sites; D024022:Fibrillar Collagens / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D009010:Monte Carlo Method; D011108:Polymers / Q000737:chemistry*; D013696:Temperature
chemical_list: D024022:Fibrillar Collagens; D011108:Polymers