ArticleProtein science : a publication of the Protein Society2004
Equilibrium thermal transitions of collagen model peptides.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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64 citing papers in PubMed.
- Light-activated thiomaleimide crosslinking stabilizes collagen mimetic peptide triple helix.Chemical communications (Cambridge, England) · 2026Article
- Influence of linker design on the stability, folding, and assembly of tethered collagen-mimetic peptides.RSC chemical biology · 2026Article
- β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.Chembiochem : a European journal of chemical biology · 2025Article
- Insights into the dual nature of αB-crystallin chaperone activity from the p.P39L mutant at the N-terminal region.Scientific reports · 2024Article
- Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing.Foods (Basel, Switzerland) · 2023Article
- A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin.The Journal of biological chemistry · 2023Article
- Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps.Angewandte Chemie (International ed. in English) · 2023Article
- Discovering design principles of collagen molecular stability using a genetic algorithm, deep learning, and experimental validation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- ColGen: An end-to-end deep learning model to predict thermal stability of de novo collagen sequences.Journal of the mechanical behavior of biomedical materials · 2022Article
- Formation of Microcages from a Collagen Mimetic Peptide via Metal-Ligand Interactions.Molecules (Basel, Switzerland) · 2021Article
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- Structural and functional studies of D109A human αB-crystallin contributing to the development of cataract and cardiomyopathy diseases.PloS one · 2021Article
- Poly(POG)n loaded with recombinant human bone morphogenetic protein-2 accelerates new bone formation in a critical-sized bone defect mouse model.Journal of orthopaedic surgery and research · 2020Article
- Temperature-controlled electrospray ionization mass spectrometry as a tool to study collagen homo- and heterotrimers.Chemical science · 2019Article
- The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.Protein science : a publication of the Protein Society · 2019Article
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- Article
- How electrostatic networks modulate specificity and stability of collagen.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Synthesis and characterization of a photocleavable collagen-like peptide.Organic & biomolecular chemistry · 2018Article
- Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.The Journal of biological chemistry · 2016Article
4 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
The folding of collagen in vitro is very slow and presents difficulties in reaching equilibrium, a feature that may have implications for in vivo collagen function. Peptides serve as good model systems for examining equilibrium thermal transitions in the collagen triple helix. Investigations were carried out to ascertain whether a range of synthetic triple-helical peptides of varying sequences can reach equilibrium, and whether the triple helix to unfolded monomer transition approximates a two-state model. The thermal transitions for all peptides studied are fully reversible given sufficient time. Isothermal experiments were carried out to obtain relaxation times at different temperatures. The slowest relaxation times, on the order of 10-15 h, were observed at the beginning of transitions, and were shown to result from self-association limited by the low concentration of free monomers, rather than cis-trans isomerization. Although the fit of the CD equilibrium transition curves and the concentration dependence of T(m) values support a two-state model, the more rigorous comparison of the calorimetric enthalpy to the van't Hoff enthalpy indicates the two-state approximation is not ideal. Previous reports of melting curves of triple-helical host-guest peptides are shown to be a two-state kinetic transition, rather than an equilibrium transition.
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