LrgpV1, Istex, Corpus, bibRecord, 000779

Synthesis, crystal structure and molecular conformation of the tBuCO‐D,L‐Ala‐Δz‐Phe‐NhiPr α,β‐unsaturated dipeptide

Identifieur interne : 000779 ( Istex/Corpus ); précédent : 000778; suivant : 000780

Synthesis, crystal structure and molecular conformation of the tBuCO‐D,L‐Ala‐Δz‐Phe‐NhiPr α,β‐unsaturated dipeptide

Auteurs : Andre Aubry ; Grzegorz Pietrzynski ; Barbara Rzeszotarska ; Guy Boussard ; Michel Marraud

Source :

International Journal of Peptide and Protein Research [ 0367-8377 ] ; 1991-01.

RBID : ISTEX:59108CAF214FE7336788EA73B501AFB1CEC349B9

English descriptors

Abstract

The crystal structure of the tBuCO‐d,l‐Ala‐Δz‐Phe‐NHiPr dipeptide has been solved by X‐ray diffraction. The peptide crystallizes in monoclinic space group P2JC with a = 13.445 (3) Å, b = 35.088 (4) Å, c = 14.755(3) Å, β= 116.73(1)°, Z = 12 and dc= 1.151 g.cm−3. The three independent molecules per asymmetric unit accommodate a βII‐folded conformation, but only one of them contains the typical i + 3 → i interaction characterizing a β‐turn. In the other two molecules, the N…O distance exceeds 3.2 Å, a value generally considered the upper limit for hydrogen bonds in peptides. In solution, the βII‐turn conformation is largely predominant.

Url:

https://api.istex.fr/document/59108CAF214FE7336788EA73B501AFB1CEC349B9/fulltext/pdf

DOI: 10.1111/j.1399-3011.1991.tb00731.x

Links to Exploration step

ISTEX:59108CAF214FE7336788EA73B501AFB1CEC349B9

Le document en format XML

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<titleGroup><title type="main">Synthesis, crystal structure and molecular conformation of the tBuCO‐D,L‐Ala‐Δ<sup>z</sup>
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<abstractGroup><abstract type="main" xml:lang="en"><p>The crystal structure of the tBuCO‐<sc>d,l</sc>
‐Ala‐Δ<sup>z</sup>
‐Phe‐NHiPr dipeptide has been solved by X‐ray diffraction. The peptide crystallizes in monoclinic space group P2JC with a = 13.445 (3) Å, b = 35.088 (4) Å, c = 14.755(3) Å, β= 116.73(1)°, Z = 12 and d<sub>c</sub>
= 1.151 g.cm<sup>−3</sup>
. The three independent molecules per asymmetric unit accommodate a βII‐folded conformation, but only one of them contains the typical i + 3 → i interaction characterizing a β‐turn. In the other two molecules, the N…O distance exceeds 3.2 Å, a value generally considered the upper limit for hydrogen bonds in peptides. In solution, the βII‐turn conformation is largely predominant.</p>
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<abstract lang="en">The crystal structure of the tBuCO‐d,l‐Ala‐Δz‐Phe‐NHiPr dipeptide has been solved by X‐ray diffraction. The peptide crystallizes in monoclinic space group P2JC with a = 13.445 (3) Å, b = 35.088 (4) Å, c = 14.755(3) Å, β= 116.73(1)°, Z = 12 and dc= 1.151 g.cm−3. The three independent molecules per asymmetric unit accommodate a βII‐folded conformation, but only one of them contains the typical i + 3 → i interaction characterizing a β‐turn. In the other two molecules, the N…O distance exceeds 3.2 Å, a value generally considered the upper limit for hydrogen bonds in peptides. In solution, the βII‐turn conformation is largely predominant.</abstract>
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<topic>βII‐turn</topic>
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Synthesis, crystal structure and molecular conformation of the tBuCO‐D,L‐Ala‐Δz‐Phe‐NhiPr α,β‐unsaturated dipeptide

Synthesis, crystal structure and molecular conformation of the tBuCO‐D,L‐Ala‐Δz‐Phe‐NhiPr α,β‐unsaturated dipeptide

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