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H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate

The conformation of the title tripeptide methyl ester hydro­chloride monohydrate, 1-[2-(methoxycarbonylmethylaminocarbonyl)pyrrolidin-1-ylcarbonyl]-2-phenylethanaminium chloride monohydrate, C(17)H(24)N(3)O(4) (+)·Cl(−)·H(2)O, is extended, but the structure cannot be classified as any typical second...

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Detalles Bibliográficos
Autores principales: Doi, Mitsunobu, Ichimiya, Yuko, Asano, Akiko
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2961031/
https://www.ncbi.nlm.nih.gov/pubmed/21202095
http://dx.doi.org/10.1107/S160053680800528X
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author Doi, Mitsunobu
Ichimiya, Yuko
Asano, Akiko
author_facet Doi, Mitsunobu
Ichimiya, Yuko
Asano, Akiko
author_sort Doi, Mitsunobu
collection PubMed
description The conformation of the title tripeptide methyl ester hydro­chloride monohydrate, 1-[2-(methoxycarbonylmethylaminocarbonyl)pyrrolidin-1-ylcarbonyl]-2-phenylethanaminium chloride monohydrate, C(17)H(24)N(3)O(4) (+)·Cl(−)·H(2)O, is extended, but the structure cannot be classified as any typical secondary structure. Interactions through water molecules and chloride ions were formed, in addition to peptide–peptide hydrogen bonds, stabilizing the molecular packing. In comparison with the previous β-turn structure of the Phe–d-Pro–Gly analogue [Doi, Ichimiya & Asano (2007 ▶). Acta Cryst. E63, o4691], it was suggested that the difference between the chiralities of Phe and Pro residues of the title compound is important to induce the β-turn structure.
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spelling pubmed-29610312010-12-30 H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate Doi, Mitsunobu Ichimiya, Yuko Asano, Akiko Acta Crystallogr Sect E Struct Rep Online Organic Papers The conformation of the title tripeptide methyl ester hydro­chloride monohydrate, 1-[2-(methoxycarbonylmethylaminocarbonyl)pyrrolidin-1-ylcarbonyl]-2-phenylethanaminium chloride monohydrate, C(17)H(24)N(3)O(4) (+)·Cl(−)·H(2)O, is extended, but the structure cannot be classified as any typical secondary structure. Interactions through water molecules and chloride ions were formed, in addition to peptide–peptide hydrogen bonds, stabilizing the molecular packing. In comparison with the previous β-turn structure of the Phe–d-Pro–Gly analogue [Doi, Ichimiya & Asano (2007 ▶). Acta Cryst. E63, o4691], it was suggested that the difference between the chiralities of Phe and Pro residues of the title compound is important to induce the β-turn structure. International Union of Crystallography 2008-03-12 /pmc/articles/PMC2961031/ /pubmed/21202095 http://dx.doi.org/10.1107/S160053680800528X Text en © Doi et al. 2008 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Organic Papers
Doi, Mitsunobu
Ichimiya, Yuko
Asano, Akiko
H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate
title H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate
title_full H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate
title_fullStr H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate
title_full_unstemmed H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate
title_short H–d-Phe–d-Pro–Gly methyl ester hydro­chloride monohydrate
title_sort h–d-phe–d-pro–gly methyl ester hydro­chloride monohydrate
topic Organic Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2961031/
https://www.ncbi.nlm.nih.gov/pubmed/21202095
http://dx.doi.org/10.1107/S160053680800528X
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