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Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3

โœ 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

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## Abstract Interpreting the data of Kobayashi et al.^1^ on the thermal transitions of triple helices of (glyโ€proโ€pro)~__n__~ for __n__ = 10, 15, and 20 using a simple model of unzippering and chain dissociation, the thermodynamic parameters characterizing glyโ€proโ€pro tripleโ€helix formation have be

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## Abstract A theoretical analysis is given of the tripleโ€helixโ€“randomโ€coil transition in a mixed solution of poly(Proโ€Proโ€Gly)~__n__~ with two different but defined degrees of polymerization __n__ and __n__โ€ฒ. Because of the highly cooperative nature of this helixโ€“coil transition, each polypeptide

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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