期刊
ORGANIC LETTERS
卷 7, 期 13, 页码 2619-2622出版社
AMER CHEMICAL SOC
DOI: 10.1021/ol050780m
关键词
-
资金
- NCRR NIH HHS [S10 RR04981] Funding Source: Medline
- NIAMS NIH HHS [AR44276] Funding Source: Medline
- NIGMS NIH HHS [GM44783] Funding Source: Medline
Collagen is the most abundant protein in animals. Interstrand N-(HO)-O-...=C hydrogen bonds between backbone amide groups form a ladder in the middle of the collagen triple helix. Isosteric replacement of the hydrogen-bond-donating amide with an ester or (E)-alkene markedly decreases the conformational stability of the triple helix. Thus, this recurring hydrogen bond is critical to the structural integrity of collagen. In this context, an ester isostere confers more stability than does an (E)-alkene.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据