Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape
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.
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
Royal Society of Chemistry
2009
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| Sorozat: | CHEMICAL COMMUNICATIONS
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| doi: | 10.1039/b812114a |
| mtmt: | 1155933 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/7557 |
| Tartalmi kivonat: | 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. |
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| Terjedelem/Fizikai jellemzők: | 177-179 |
| ISSN: | 1359-7345 |