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Characterization of collagen‐like heterotrimers: Implications for triple‐helix stability
Author(s) -
Berisio Rita,
Granata Vincenzo,
Vitagliano Luigi,
Zagari Adriana
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20017
Subject(s) - triple helix , collagen helix , chemistry , hydroxylation , hydroxyproline , helix (gastropod) , proline , stereochemistry , biophysics , biochemistry , amino acid , enzyme , biology , ecology , snail
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