Hetényi, Anasztázia and Szakonyi, Zsolt and Mándity, István and Szolnoki, Éva Tünde and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc (2009) Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape. CHEMICAL COMMUNICATIONS (2). pp. 177-179. ISSN 1359-7345
|
Text
10.1039B812114A_u.pdf Download (600kB) | Preview |
Official URL: http://dx.doi.org/10.1039/b812114a
Abstract
The long-range side-chain repulsion between the (1R, 2R, 3R, 5R)-2- amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers.
| Item Type: | Article |
|---|---|
| Subjects: | Q Science / természettudomány > QD Chemistry / kémia |
| SWORD Depositor: | MTMT SWORD |
| Depositing User: | MTMT SWORD |
| Date Deposited: | 10 Jun 2016 12:58 |
| Last Modified: | 10 Jun 2016 12:58 |
| URI: | http://real.mtak.hu/id/eprint/36252 |
Actions (login required)
 |
Edit Item |
