Sculpting the β-peptide foldamer H12 helix via a designed side-chain shape
- 14 November 2008
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- No. 2,p. 177-179
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 β-peptide oligomers.Keywords
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