## Abstract Relevant parameters and stereochemical consequences of helices [α‐helix, 3~10~‐helix, β‐bend ribbon spiral, γ‐helix, 2.0~5~‐helix, poly(Pro)~__n__~ type‐I and ‐II helices, and collagen triple helix] of peptides based on α‐amino acids for use as templates in various branches of chemistry
On the band gap in peptide α-helices
✍ Scribed by Thomas Herz; Peter Otto; Timothy Clark
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 191 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0020-7608
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A ngeles, Los A nge les, California 90024 ## Synopsis Solvent accessible peptide bonds in proteins exhibit a 1-3" compression of the OCN bond angle and a corresponding expansion of the NCCa bond angle, relative to buried peptide bonds. These changes are consistent with an increase in hydrogen bon
It was previously found that a cationic amphiphilic peptide, Ac-(Leu-Ala-Arg-Leu) 3 -NHCH 3 (4 3 ), caused the destabilization of a phospholipid membrane and showed strong antibacterial activity [Lee et al. Biochim. Biophys. Acta 1986; 862: 211 -219]. In order to investigate the effect of changing h