title: Macrocyclic scaffold for the collagen triple helix.
abstract: [structure: see text] Three strands of natural collagen are linked by covalent bonds prior to their folding into a triple helix. We report on a synthetic collagen in which the strands are pendent on a rigid macrocyclic scaffold of C(3) symmetry. The scaffold confers substantial conformational stability upon the collagen triple helix and makes its folding independent of concentration, both desirable attributes for exploring and exploiting synthetic collagens.
authors.affiliation: Departments of Biochemistry and Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
authors.forename: Jia-Cherng
authors.initials: JC
authors.lastname: Horng
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Hawk
authors.forename: Qian
authors.initials: Q
authors.lastname: Zhao
authors.forename: Eric S
authors.initials: ES
authors.lastname: Benedict
authors.forename: Steven D
authors.initials: SD
authors.lastname: Burke
authors.forename: Ronald T
authors.initials: RT
authors.lastname: Raines
mesh_terms: D000595:Amino Acid Sequence; D003094:Collagen / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D003094:Collagen