Conformationally constrained amino acid and dipeptide units can serve in mimics of specific secondary structures for studying relationships between peptide conformation and biological activity. A variety of mimics are required to study systematically the structure-activity relationships in biologica
Unsaturated amino-acid residues as probes for the conformation of polypeptides in solution
✍ Scribed by Osvaldo Pieroni; Adriano Fissi; Giorgio Montagnoli; Francesco Ciardelli
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1977
- Tongue
- English
- Weight
- 479 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Acetyl‐(dehydro‐Phe) and acetyl‐bis(dehydro‐Phe) groups have been attached to the ε‐amino group of the lysine residues of the copolymer poly(Glu^92^Lys^8^) by reacting this last with acetyl‐(dehydro‐Phe)‐azlactone and acetyl‐bis(dehydro‐Phe)‐azlactone, respectively.
In the latter case induced CD is observed between 250 and 330 nm, due to the relative dissymmetric disposition of the two dehydro‐Phe groups under the chiral field of the polypeptide chain.
pH dependence of the induced CD, observed for the copolymer and lacking in the lowmolecular‐weight structural model, is related to the α‐helical and random coiled conformation of the polypeptide chain.
📜 SIMILAR VOLUMES
## Abstract The ^13^C chemical shifts and spin‐lattice relaxation times are reported for __cyclo__(L‐Pro‐L‐Leu) and __cyclo__(L‐Pro‐D‐Leu). The chemical shifts of the D and L leucyl residues in the cyclic peptides differ from each other by 1.8 and 3.6 parts per million for the α and β carbons, resp
The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.