ArticleBiochemistry2015
Dynamic Water-Mediated Hydrogen Bonding in a Collagen Model Peptide.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- Injectable Sodium Hyaluronate Hydrogels Modified by Ionic and Nonionic Polymers Loaded with Prednisolone Disodium Phosphate: Molecular Interactions and Intra-Articular Drug Delivery.International journal of molecular sciences · 2026Article
- Unraveling and Sliding of Polypeptide Strands Underlies the Exceptional Toughness of the Triple-Helix Collagen Molecule.ACS nano · 2026Article
- How Hydration Weakens Collagen: A Mesoscale Energy Decomposition of Type I and Type II Fibrils.Computational and structural biotechnology journal · 2026Article
- L-Serine-Incorporated Collagen Scaffolds for Modulating In Vivo Degradation Behavior.Journal of functional biomaterials · 2025Article
- Photosensitive small intestinal submucosal hydrogels loaded with the KR-12-a5 peptide promote periodontal osteogenesis and antimicrobial activity.Journal of nanobiotechnology · 2025Article
- Nanoscale Structural and Functional Impacts of Disease-Associated Collagen Mutations.bioRxiv : the preprint server for biology · 2025Article
- Progress in Research on Animal Collagen Peptides: Preparation, Bioactivity, and Application.Molecules (Basel, Switzerland) · 2025Review
- Water and Collagen: A Mystery Yet to Unfold.Biomacromolecules · 2025Review
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Biomolecules · 2022Article
- Mechanistic Insights into the Structural Stability of Collagen-Containing Biomaterials Such as Bones and Cartilage.The journal of physical chemistry. B · 2021Article
- Using quantum chemistry to estimate chemical shifts in biomolecules.Biophysical chemistry · 2020Review
- The Construction of Biomimetic Cementum Through a Combination of Bioskiving and Fluorine-Containing Biomineralization.Frontiers in bioengineering and biotechnology · 2020Article
- Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding.Protein science : a publication of the Protein Society · 2016Article
- Importance of the Linker Region in Matrix Metalloproteinase-1 Domain Interactions.RSC advances · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In the canonical (G-X-Y)(n) sequence of the fibrillar collagen triple helix, stabilizing direct interchain hydrogen bonding connects neighboring chains. Mutations of G can disrupt these interactions and are linked to connective tissue diseases. Here we integrate computational approaches with nuclear magnetic resonance (NMR) to obtain a dynamic view of hydrogen bonding distributions in the (POG)(4)(-)(POA)-(POG)(5) peptide, showing that the solution conformation, dynamics, and hydrogen bonding deviate from the reported X-ray crystal structure in many aspects. The simulations and NMR data provide clear evidence of inequivalent environments in the three chains. Molecular dynamics (MD) simulations indicate direct interchain hydrogen bonds in the leading chain, water bridges in the middle chain, and nonbridging waters in the trailing chain at the G → A substitution site. Theoretical calculations of NMR chemical shifts using a quantum fragmentation procedure can account for the unusual downfield NMR chemical shifts at the substitution sites and are used to assign the resonances to the individual chains. The NMR and MD data highlight the sensitivity of amide shifts to changes in the acceptor group from peptide carbonyls to water. The results are used to interpret solution NMR data for a variety of glycine substitutions and other sequence triplet interruptions to provide new connections between collagen sequences, their associated structures, dynamical behavior, and their ability to recognize collagen receptors.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.