Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Triple-helical peptides: an approach to collagen conformation, stability, and self-association.

Biopolymers - 1 May 2008

Brodsky Barbara, Thiagarajan Geetha, Madhan Balaraman, Kar Karunakar

Abstract excerpt

Peptides have been an integral part of the collagen triple-helix structure story, and have continued to serve as useful models for biophysical studies and for establishing biologically important sequence-structure-function relationships. High resolution structures of triple-helical peptides have confirmed the basic Ramachandran triple-helix model and provided new insights into the hydration, hydrogen bonding, and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Collagen
Share to Crystallography, X-Ray
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Models, Biological

Share to Models, Molecular

Share to Peptides

Share to Protein Conformation

Source

Identifiers

PMID: 18275087
DOI: 10.1002/bip.20958

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Triple-helical peptides: an approach to collagen conformation, stability, and self-association.PMID 18275087Read ↗

Disrupted collagen architecture in the crystal structure of a triple-helical peptide with a Gly-->Ala substitution.Semantic proximity Read ↗

A Collagen Triple Helix without the Super Helical TwistSemantic proximity Read ↗

Thermostability gradient in the collagen triple helix reveals its multi-domain structure.Semantic proximity Read ↗

Designed triple-helical peptides as tools for collagen biochemistry and matrix engineeringSemantic proximity Read ↗

Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine.Semantic proximity Read ↗

Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.Semantic proximity Read ↗

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.Semantic proximity Read ↗

Prediction of collagen stability from amino acid sequence.Semantic proximity Read ↗

Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Semantic proximity Read ↗

Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases.Semantic proximity Read ↗

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged SiteSemantic proximity Read ↗

Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.