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  • 1975-1979  (3)
  • Polymer and Materials Science  (3)
  • allelochemical
  • 1
    Digitale Medien
    Digitale Medien
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 1 (1975), S. 227-234 
    ISSN: 0025-116X
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie , Physik
    Beschreibung / Inhaltsverzeichnis: IR-spektroskopische Untersuchungen von Polyäthylen-Proben, dargestellt durch Reduktion von Polyvinylchlorid mit Lithiumaluminiumhydrid, ließen darauf schließen, daß Polyvinylchlorid Seitenketten enthält, die seine Morphologie und Festkörpereigenschaften wesentlich beeinflussen. Die Natur dieser Seitenketten war bisher unbekannt. Es wird anhand von 13C-NMR Spektren gezeigt, daß die Verzweigungen in reduziertem Polyvinylchlorid aus Methylgruppen bestehen, die vermutlich aus Chlormethylgruppen des ursprünglichen Polymeren entstanden sind. Die untersuchte Probe enthielt ca. 3 CH3-Gruppen pro 1000 CH2-Gruppen, jedoch is dieses Verhältnis vermutlich von der Polymerisationstemperatur abhängig. Zusätzlich wurden Anzeichen für längere Seitenketten gefunden, die allerdings nur in einem Ausmaß von weniger als 1 pro 1000 CH2-Gruppen vorhanden sein dürften.
    Notizen: The presence of branches in poly(vinyl chloride) as indicated by previous IR measurements on the polymer reduced to polyethylene by means of lithium aluminum hydride is believed to affect materially the morphology and solid state properties of poly(vinyl chloride); however, up to the present, the nature of these branches has not been known. By use of 13C-NMR on reduced poly(vinyl chloride) it is demonstrated that the brances are methyl groups, presumably corresponding to chloromethyl groups in the original polymer. In the sample studied, the frequency is ca. 3 methyl groups per 1000 CH2 groups, but this is expected to depend on the temperature of polymerization. There is also some evidence for long branches, probably not exceeding 1 per 1000 CH2 groups.
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York : Wiley-Blackwell
    Biopolymers 14 (1975), S. 987-997 
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The C2H resonance of the active site histidine residue designated AS-2, which has the lower pKa of the two active site histidines, has been correlated in both RNase A and RNase S by comparing the pH 3 to 5.5 regions of the chemical shift titration curves, the effect of the inhibitor CMP-3′ on the chemical shifts at pH 4.0, and the effect of Cu II on the line widths at pH 3.6. It has been demonstrated that resonance AS-2 is absent in the spectrum of RNase S′ reconstituted using S-peptide deuterated at the C2 of His 12, and in that of the RNase S′-CMP-3′ complex. We thus demonstrate that histidine AS-2 is in fact His 12 in both enzymes. This finding is in agreement with out previous assignment of the exchangeable NH proton in RNase A to His 12, but reverses the assignments of the active site histidine C2H resonances made earlier by other authors.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Described herein are proton nmr experiments on chemically modified derivatives of ribonuclease A designed to elucidate the origin of an exchangeable resonance, assigned previously to a histidine ring N proton that titrates between 11 to 13 ppm with a pKa of 6.1 in H2O solution. Histidines 48 and 105, which are distant from the active site, are eliminated as candidates for this resonance from inhibitor binding studies on the enzyme in acetate-water solutions. This exchangeable resonance titrates with modified pKa's and constant area over the above pH range in His-119-N1-carboxymethylated-RNase A and des-(121-124)-RNase A, thus eliminating the imidazole N3 proton in the His 119-Asp 121 hydrogen bond. In His-12-N1-carboxymethylated-RNase A, this resonance is also observable, but broadens on raising the pH above 7 and at elevated temperatures above neutrality. It exhibits a pH-independent chemical shift characteristic of the protonated state of histidine. On the basis of these findings, this exchangeable resonance, designated a, is assigned to the imidazole N1 proton of His 12, which is hydrogen-bonded to the carbonyl oxygen of Thr 45 in the crystal.
    Zusätzliches Material: 6 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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