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Article

Thermostability gradient in the collagen triple helix reveals its multi-domain structure.

Journal of molecular biology - 14 May 2004

Steplewski Andrzej, Majsterek Ireneusz, McAdams Erin, Rucker Eileen, Brittingham Raymond J, Ito Hidetoshi, Hirai Kazuya, Adachi Eijiro, Jimenez Sergio A, Fertala Andrzej

Abstract excerpt

A triple-helical conformation and stability at physiological temperature are critical for the mechanical and biological functions of the fibril-forming collagens. Here, we characterized the role of consecutive domains of collagen II in stabilizing the triple helix. Analysis of melting temperatures of genetically engineered collagen-like proteins consisting of tandem repeats of the D1, D2, D3 or D4 collagen II...

Topics

Blotting, Western
Circular Dichroism
Collagen
Electrophoresis
Mutation
Procollagen
Protein Structure, Quaternary
Protein Structure, Tertiary
Sequence Analysis, Protein
Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15111062
DOI: 10.1016/j.jmb.2004.03.037

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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