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Characterization of collagen-like heterotrimers: Implications for triple-helix stability

✍ Scribed by Rita Berisio; Vincenzo Granata; Luigi Vitagliano; Adriana Zagari

Publisher
Wiley (John Wiley & Sons)
Year
2004
Tongue
English
Weight
445 KB
Volume
73
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

This article deals with the effects of proline hydroxylation on collagen triple‐helix stability, an issue that is still under discussion. To investigate the structural determinants of triple‐helix stabilization by hydroxyproline (Hyp), we here characterized spectroscopically triple‐helix heterotrimers containing both chains of (Pro–Pro–Gly)~10~ and (Pro–Hyp–Gly)~10~. Results are discussed in relation to the various triple‐helix stabilization mechanisms. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004

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