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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Monatshefte für Chemie 103 (1972), S. 1604-1612 
    ISSN: 1434-4475
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Die Bereitung und die Charakterisierung der ersten Elemente der Folge (Ala x−Glyy)n wird fürx=1 oder 2,y=1, 2 oder 3, undx=3,y=3, beschrieben. Das spektroskopische und kristallographische Studium dieser Polymeren im festen Zustand beweist, daß sie in zwei kristallinischen Formen vorliegen können; sie haben durchwegs β-Konformation. Wennx verschieden vony ist, nimmt das Polymere — mit Ausnahme von (Ala 2−Gly3)n — die gewöhnliche Konformation des Restes, der im Überschuß ist, an. Zum Beispiel haben wir für (Ala−Gly 2)n und (Ala−Gly 3)n die Existenz einer Konformation bewiesen, die der II-Form der Polyglycine nahekommt. Wennx=y=1, bildet das Polymere eine besondere Form, deren konformationelle Periode die peptidische Einheit ist, und die große Ähnlichkeiten mit der löslichen Form der Seide vom Bombyx Mori zeigt. Diese Ergebnisse illustrieren das Interesse, das den synthetischen Polypeptiden als Modellen für das Studium der Faserproteine, wie der Seiden, zukommt.
    Notes: Abstract Polypeptides of the type (Ala x−Glyy)n) with a periodic distribution ofl-alanyl and glycyl residues i.e. poly (Ala−Gly), poly(Ala−Gly 2), poly(Ala−Gly 3), poly(Ala 2 −Gly), poly(Ala 2 −Gly 2), poly(Ala 2 −Gly 3), and poly(Ala 3 −Gly 3) were synthetized by polymerization of the corresponding peptide pentachlorophenyl ester in benzene. Depending on the work up the ensuing polypeptides may exist in the solid state under two different conformations characterized by I.R.-spectroscopy, circular dichroism and X-ray diffraction. All exibit the β structure. In addition of this, whenx is different fromy, the polymer assumes the usual conformation of the residue which is predominant. For instance, we show that poly(Ala−Gly 2) and poly(Ala−Gly 3) possess a polyglycine II type structure. Ifx=y=1, the polymer shows a particular structure characterized by a dipeptide conformational unit resembling the water soluble form of silk from Bombyx mori. These results show the interest of synthetic periodic polypeptides as models for fibrous proteins like silks.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1075-2617
    Keywords: biosurfactant ; lipopeptide ; surfactins ; Bacillus subtilis ; NMR ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The biosynthesis of bacterial isoleucyl-rich surfactins was controlled by supplementation of L-isoleucine to the culture medium. Two new variants, the [Ile4,7]- and [Ile2,4,7]surfactins, were thus produced by Bacillus subtilis and their separation was achieved by reverse-phase HPLC. Amino acids of the heptapeptide moiety were analysed by chemical methods, and the lipid moiety was identified to β-hydroxy anteiso pentadecanoic acid by combined GC/MS. Sequences were established on the basis of two-dimensional NMR data. Because conformational parameters issuing from NMR spectra suggested that the cyclic backbone fold was globally conserved in the new variants, structure-activity relationships were discussed in details on the basis of the three-dimensional model of surfactin in solution. Indeed, both variants have increased surface properties compared with that of surfactin, and this improvement is assigned to an increase of the hydrophobicity of the apolar domain favouring micellization. Furthermore, the additional Leu-to-Ile substitution at position 2 in the [Ile2,4,7]surfactin leads to a substantial increase of its affinity for calcium, when compared with that of [Ile4,7]surfactin or surfactin. This effect is assigned, from the model, to an increase in the accessibility of the acidic side chains constituting the calcium binding site. Thus, the propensities of such active lipopeptides for both hydrophobic and electrostatic interactions were improved, further substantiating that they can be rationally designed. © 1997 European Peptide Society and John Wiley & Sons, Ltd
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 2299-2310 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Alternating poly(Arg-Leu) and copolypeptides with Arg-Leu and His-Leu sequences were prepared by condensation of the corresponding p-nitrophenyl dipeptide esters in the presence of 1-hydroxybenzotriazole. Arginine was used without any protection and histidine side chains were protected using π-benzyloxymethyl group recently introduced in peptide chemistry. The ability of these polypeptides with alternating hydrophilic and hydrophobic residues to form water-soluble β-sheets was investigated by CD.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Iturin A is a lipopeptide extracted from strains of Bacillus subtilis. Seven peptide residues form a cycle closed by a β-amino acid carrying a hydrophobic tail. This compound is an antifungal and induces the formation of conducting pores in black lipid membranes. Two-dimensional 1H-nmr was used for investigating its conformation in pyridine. A complete set of nuclear Overhauser effects (NOEs) was obtained from which interproton distances were deduced in a rather broad range of 2.2-4.2 Å. A special procedure was then used to optimize simultaneously experimental parameters and intramolecular energy calculated by semiempirical methods. A model of the conformation is proposed for the backbone for which there is an excellent coherence between NOEs, coupling constants, and intramolecular energy. The conformations of Asn, Gln, and Ser side chains appear to be much more flexible because of their interactions with the solvent. From this picture, iturin A seems to have a rather stiff ring surrounded by mobile side chains. Further studies of this lipopeptide and of other members of the family should enable us to approach some structure-activity relationships for this class of antibiotics.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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