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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of organic chemistry 27 (1962), S. 679-682 
    ISSN: 1520-6904
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0091-7419
    Keywords: 1H NMR ; periplasmic binding protein ; histidine-binding protein J ; membrane transport ; pore model ; transport of L-histidine ; Salmonella typhimurium ; substrate-induced conformational changes ; deuterated amino acids ; partially deuterated protein ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Genetic evidence suggests that the high-affinity L-histidine transport in Salmonella typhimurium requires the participation of a periplasmic binding protein (histidine-binding protein J) and two other proteins (P and Q proteins). The histidine-binding protein J binds L-histidine as the first step in the high-affinity active transport of this amino acid across the cytoplasmic membrane. High-resolution proton nuclear magnetic resonance spectroscopy at 600 MHz is used to investigate the conformations of this protein in the absence and presence of substrate. Previous nuclear magnetic resonance results reported by this laboratory have shown that there are extensive spectral changes in this protein upon the addition of L-histidine. When resonances from individual amino acid residues of a protein can be resolved in the proton nuclear magnetic resonance spectrum, a great deal of detailed information about substrate-induced structural changes can be obtained. In order to gain a deeper insight into the nature of these structural changes, deuterated phenylalanine or tyrosine has been incorporated into the bacteria. Proton nuclear magnetic resonance spectra of selectively deuterated histidine-binding protein J were obtained and compared to the normal protein. Several of the proton resonances have been assigned to the various aromatic amino acid residues of this protein. A model for the high-affinity transport of L-histidine across the cytoplasmic membrane of S typhimurium is proposed. This model, which is a version of the pore model, assumes that both P and Q proteins are membrane-bound and that the interface between these two proteins forms the channel for the passage of substrate. The histidine-binding protein J serves as the “key” for the opening of the channel for the passage of L-histidine. In the absence of substrate, this channel or gate is closed owing to a lack of appropriate interactions among these three proteins. The channel can be opened upon receiving a specific signal from the “key”; namely, the substrate-induced conformational changes in the histidine-binding protein J molecule. This model is consistent with available experimental evidence for the high-affinity transport of L-histidine across the cytoplasmic membrane of S typhimurium.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Polymer Science Part A: General Papers 2 (1964), S. 4647-4659 
    ISSN: 0449-2951
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: An investigation was made of the pink-orange color that reaches maximum intensity at the midpoint of the titration of homopolymers of vinylhydroquinone. It was shown that during oxidative titration the hydroquinone absorption at 295 mμ decreases in intensity while quinone absorption at 254 mμ, increases. At the midpoint of the titration absorption at approximately 455 mμ, the pink color, reaches its maximum intensity, with relatively low extinction coefficient. The position of the maxima does not change with extent of oxidation; the specific extinction coefficient is independent of concentration and degree of polymerization, but somewhat dependent on the nature of the solvent. When the functional groups were somewhat separated along the chain by copolymerization with an alternating comonomer, styrene, α-methylstyrene, or acrylamide, there was no appreciable shift in the ultraviolet absorption peaks with oxidation, but in the visible region the intensity at 455 mμ was greatly decreased, compared with homopolymer, at all degrees of oxidation around the midpoint. Analysis of the spectroscopic data led to the conclusion that the number of quinhydronelike interactions is low relative to the number of groups that are not interacting.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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