ArticleThe Journal of biological chemistry2011
Interstrand dipole-dipole interactions can stabilize the collagen triple helix.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Collagen Prolyl 4-Hydroxylase: An Emerging Key Player in Cardiac Fibrosis.Journal of cardiovascular translational research · 2026Review
- Histological and molecular characterization of bone integrity in osteogenesis imperfecta: a case series across genetic subtypes.JBMR plus · 2026Article
- Contrasting Local and Macroscopic Effects of Collagen Hydroxylation.International journal of molecular sciences · 2021Article
- How Water in Aliphatic Solvents Directs the Interference of Chemical Reactivity in a Supramolecular System.Journal of the American Chemical Society · 2020Article
- Subwavelength hyperspectral THz studies of articular cartilage.Scientific reports · 2018Article
- Metal-Promoted Assembly of Two Collagen Mimetic Peptides into a Biofunctional "Spiraled Horn" Scaffold.Materials (Basel, Switzerland) · 2016Article
- Thioamides in the collagen triple helix.Chemical communications (Cambridge, England) · 2015Article
- Polyproline and triple helix motifs in host-pathogen recognition.Current protein & peptide science · 2012Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The amino acid sequence of collagen is composed of GlyXaaYaa repeats. A prevailing paradigm maintains that stable collagen triple helices form when (2S)-proline (Pro) or Pro derivatives that prefer the C(γ)-endo ring pucker are in the Xaa position and Pro derivatives that prefer the C(γ)-exo ring pucker are in the Yaa position. Anomalously, an amino acid sequence in an invertebrate collagen has (2S,4R)-4-hydroxyproline (Hyp), a C(γ)-exo-puckered Pro derivative, in the Xaa position. In certain contexts, triple helices with Hyp in the Xaa position are now known to be hyperstable. Most intriguingly, the sequence (GlyHypHyp)(n) forms a more stable triple helix than does the sequence (GlyProHyp)(n). Competing theories exist for the physicochemical basis of the hyperstability of (GlyHypHyp)(n) triple helices. By synthesizing and analyzing triple helices with different C(γ)-exo-puckered proline derivatives in the Xaa and Yaa positions, we conclude that interstrand dipole-dipole interactions are the primary determinant of their additional stability. These findings provide a new framework for understanding collagen stability.
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Registered trials
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