title: Control of Collagen Triple Helix Stability by Phosphorylation.
abstract: The phosphorylation of the collagen triple helix plays an important role in collagen synthesis, assembly, signaling, and immune response, although no reports detailing the effect this modification has on the structure and stability of the triple helix exist. Here we investigate the changes in stability and structure resulting from the phosphorylation of collagen. Additionally, the formation of pairwise interactions between phosphorylated residues and lysine is examined. In all tested cases, phosphorylation increases helix stability. When charged-pair interactions are possible, stabilization via phosphorylation can play a very large role, resulting inasmuch as a 13.0 °C increase in triple helix stability. Two-dimensional NMR and molecular modeling are used to study the local structure of the triple helix. Our results suggest a mechanism of action for phosphorylation in the regulation of collagen and also expand upon our understanding of pairwise amino acid stabilization of the collagen triple helix.
authors.affiliation: Department of Chemistry, Rice University 6100 Main Street, Houston, Texas 77005, United States.
authors.forename: Amanda M
authors.initials: AM
authors.lastname: Acevedo-Jake
authors.affiliation: Department of Chemistry, Rice University 6100 Main Street, Houston, Texas 77005, United States.
authors.forename: Daniel H
authors.initials: DH
authors.lastname: Ngo
authors.affiliation: Department of Chemistry, Rice University 6100 Main Street, Houston, Texas 77005, United States.
authors.forename: Jeffrey D
authors.identifier: 0000-0002-3186-5395
authors.initials: JD
authors.lastname: Hartgerink
mesh_terms: D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010766:Phosphorylation; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D003094:Collagen