| Autor: |
Jenkins CL; Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA., Vasbinder MM, Miller SJ, Raines RT |
| Jazyk: |
angličtina |
| Zdroj: |
Organic letters [Org Lett] 2005 Jun 23; Vol. 7 (13), pp. 2619-22. |
| DOI: |
10.1021/ol050780m |
| Abstrakt: |
[structure: see text] Collagen is the most abundant protein in animals. Interstrand N-H...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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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