A guest-host approach to oligodepsipeptide structure.
| dc.contributor.author | Goodman, M | |
| dc.contributor.author | Venkatachalapathi, Y V | |
| dc.contributor.author | Mammi, S | |
| dc.contributor.author | Katakai, R | |
| dc.date.accessioned | 2015-07-22T11:58:07Z | |
| dc.date.available | 2015-07-22T11:58:07Z | |
| dc.date.issued | 1985-08 | |
| dc.description.abstract | In this paper we investigate the effect of main chain isosteric replacement of specific amino acid residues by α-hydroxy acids. As part of a long term program specifically protected heptaglutamates were prepared and their circular dichroism and nuclear magnetic resonance spectra in various solvents were examined. From these experiments conformational preferences were deduced. We have also prepared oligo-(γ-methyl-glutamates) replacing the amino acids at specific positions along the chain with S-lactic acid and have elucidated the effect of these main chain isosteric replacements on oligopeptide structure. Analogues of collagen also have been prepared with glycolic acid replacing specific glycine residues. We synthesized the model hexamers Ac-Ala-Gly-Pro-Ala-Gly-Pro-NHMe, Ac-Ala- Glc-Pro-Ala-Gly-Pro-NHMe, and Ac-Ala-Gly-Pro-Ala-Glc-Pro-NHMe in order to study their structural characteristics under various conditions. Preliminary nuclear magnetic resonance and circular dichroism results are presented. | en_US |
| dc.identifier.citation | Goodman M, Venkatachalapathi Y V, Mammi S, Katakai R. A guest-host approach to oligodepsipeptide structure. Journal of Biosciences. 1985 Aug; 8(1&2): 223-238. | en_US |
| dc.identifier.uri | https://imsear.searo.who.int/handle/123456789/160386 | |
| dc.language.iso | en | en_US |
| dc.source.uri | https://www.ias.ac.in/jarch/jbiosci/8/223-238.pdf | en_US |
| dc.subject | Oligodepsipeptides | en_US |
| dc.subject | nuclear magnetic resonance | en_US |
| dc.subject | circular dichroism | en_US |
| dc.subject | hydrogen bonding | en_US |
| dc.title | A guest-host approach to oligodepsipeptide structure. | en_US |
| dc.type | Article | en_US |