Self-association-driven transition of the beta-peptidic H12 helix to the H18 helix
Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S, 5S)-2-amino-6,6-dimethylbicyclo-[3.3.1]heptane-3-carboxylic acid) and beta(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repul...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
Royal Society of Chemistry Publishing
2012
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| Sorozat: | ORGANIC & BIOMOLECULAR CHEMISTRY
10 No. 2 |
| doi: | 10.1039/c1ob06627g |
| mtmt: | 1842289 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/7546 |
| Tartalmi kivonat: | Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S, 5S)-2-amino-6,6-dimethylbicyclo-[3.3.1]heptane-3-carboxylic acid) and beta(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repulsions attain the beta-H18 helix in CD3OH. As a close relative of the alpha-helix, this helix type is stabilized by i-i+4 backbone H-bond interactions. The formation of the beta-H18 helix was found to be solvent-and concentration-dependent. Upon dilution, the beta-H18 -> beta-H12 helix transition was revealed by concentration-dependent ECD, DOSY-NMR and TEM measurements. |
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| Terjedelem/Fizikai jellemzők: | 255-259 |
| ISSN: | 1477-0520 |