## Abstract The synthesis and characterization of a series of oligopeptides (from the tripeptide to the octadecapeptide) with the repeating sequence L‐norvalyl‐glycyl‐L‐proline and a polytripeptide with this sequence are reported. The oligomers were synthesized step by step using the mixed anhydrid
Sequential oligopeptides. Conformational studies of the oligopeptides and a polypeptide with the repeating sequence L-norvalyl-glycyl-L-proline
✍ Scribed by Gian Maria Bonora; Claudio Toniolo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 527 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Conformational studies of a series of oligopeptides (from the tripeptide to the octadecapeptide) with the repeating sequence L‐norvalyl‐glycyl‐L‐proline and a polytripeptide with this sequence are reported. By means of chiroptical techniques, unordered conformations are found for all oligopeptides in water, trifluoroethanol, and ethylene glycol and for the water‐insoluble polymer in trifluoroethanol. In ethylene glycol the polymer assumes a collagen‐like structure. Infrared studies indicate that all the oligomers, in contrast to the polymer, are unordered in the solid state.
📜 SIMILAR VOLUMES
## Abstract A series of sequential oligopeptides having simple nonpolar side chains, Nps‐(L‐Ala‐L‐Leu‐Gly)~__n__~‐ OEt has been prepared by a stepwise fragment‐condensation method using Nps‐L‐alanyl‐L‐leucylglycine __N__‐hydroxysuccinimide ester, which was prepared by the Nps‐__N__‐carboxy α‐amino‐
## Abstract The circular dichroic properties of H‐Gly‐Phe‐(Gly)~__n__~‐Trp‐Gly‐OH (II, __n__ = 0,1,2) and of related simpler peptides, such as H‐Phe‐Gly‐OH, H‐Gly‐Phe‐OH, H‐Gly‐Phe‐Gly‐OH, H‐Phe‐Trp‐OH, H‐Phe‐Trp‐Gly‐OH, and H‐Gly‐Phe‐Trp‐OH in water and trifluoroethanol solutions are investigated.