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

被引：18
作者：
Berisio, R
Granata, V
Vitagliano, L
Zagari, A
机构：
[1] CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy
[2] Univ Naples, Dipartimento Chim Biol, I-80134 Naples, Italy
来源：
BIOPOLYMERS | 2004年 / 73卷 / 06期
关键词：
collagen; heterotrimers; protein stability; protein denaturation; hydroxyproline; CD; polypeptide models;
D O I：
10.1002/bip.20017
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2004 Wiley Periodicals, Inc.
引用
收藏
页码：682 / 688
页数：7
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