## Abstract Interpreting the data of Kobayashi et al.^1^ on the thermal transitions of triple helices of (glyโproโpro)~__n__~ for __n__ = 10, 15, and 20 using a simple model of unzippering and chain dissociation, the thermodynamic parameters characterizing glyโproโpro tripleโhelix formation have be
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
โ Scribed by Rita Berisio; Luigi Vitagliano; Lelio Mazzarella; Adriana Zagari
- Book ID
- 111753336
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2009
- Tongue
- English
- Weight
- 830 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0961-8368
- DOI
- 10.1110/ps.32602
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Abstract A theoretical analysis is given of the tripleโhelixโrandomโcoil transition in a mixed solution of poly(ProโProโGly)~__n__~ with two different but defined degrees of polymerization __n__ and __n__โฒ. Because of the highly cooperative nature of this helixโcoil transition, each polypeptide
Measurements of the molecular weight of (Pro-Pro-Gly), and (Pro-Pro-Gly),(Ala-Pro-Gly),(Pro-Pro-Gly),, which were synthesized by the solid-phase method, revealed that they formed a trimer in an aqueous solution, and dissociated into single-stranded chains on warming. Accompanying the transition, a l