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  • 1
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    Biochemistry 33 (1994), S. 6850-6858 
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    Journal of the American Chemical Society 117 (1995), S. 4448-4454 
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 99 (1995), S. 13352-13355 
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 9819-9825 
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 5
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Substance P (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2), a neuromodulator involved in the transmission of pain information, exerts its biological effects by binding to membrane-embedded protein receptors. The influence of membrane lipids on neuropeptide conformation may be critical to these processes. We have characterized in detail the complexes formed between substance P and sodium dodecylsulfate (SDS), lysophosphatidylglycerol, and lysophosphatidylcholine micelles. CD spectra of substance P displayed significant induced secondary structure upon addition of these lipids. Potentiometric titration data demonstrated that the pKa of the peptide N-terminal amino group increased from ca. 7.0 to 9.0 in SDS-bound substance P, suggesting direct interaction of the substance P N-terminus with the lipid head-group region. Red shifts in uv spectra of the Phe rings in membrane-bound peptide suggested an increased hydrophobic environment for these substituents. High-resolution one- and two-dimensional correlated spectroscopy nmr spectra displayed differential chemical-shift movements of substance P Gln, Leu, and Met NH protons with added lipid, suggesting involvement of the C-terminal portion of the peptide in the induced secondary structure. The clear influence of the lipid environment on the substance P conformational ensemble suggests a role for the membrane in the events leading to receptor binding.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    New York : Wiley-Blackwell
    Biopolymers 29 (1990), S. 149-157 
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Although noted as hydrophilic residues with helix-breaking potential, proline residues are observed in putatively α-helical transmembrane (TM) segments of many channel-forming integral membrane proteins. In addition to the recognized property of X-Pro peptide bonds (where X = any amino acid) to occur in cis as well as trans isomeric states, the tertiary amide character of the X-Pro bond confers increased propensity for involvement of its carbonyl group in specific H-bonded structures (e.g., β- and γ-turns) and/or liganding interactions with positively charged species. To examine this latter situation in further detail, we identified Leu-Pro-Phe as a consensus sequence triad based on actual occurrences of intramembranous Pro residues in transport protein TM segments. Accordingly, we have undertaken the synthesis of hydrophobic peptides with potential membrane affinity, of which t-butyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Pro-L-Phe-OH (t-Boc-AAALPF-OH) is an initial compound. Partitioning of this peptide into model membrane environments composed of lipid micelles induces specific conformations(s) for the membrane-bound hexapeptide, as monitored by 75-MHz 13C-nmr spectral behavior of 13C-enriched Leu and Pro carbonyl carbons, and by 300-MHz 1H-nmr spectra of peptide α, β, and aromatic protons. Data are interpreted in terms of an intramolecularly H-bonded inverse γ-turn conformation in the membrane environment involving the Leu-Pro-Phe triad. The inherent structureal instability of a Pro-containing segment in a TM helix due to the multiplicity of possible local conformations is discussed as a functional aspect of membrane-buried prolines in transport proteins.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 7
    Digitale Medien
    Digitale Medien
    New York : Wiley-Blackwell
    Biopolymers 28 (1989), S. 267-272 
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: A membrance potential is shown to be established in phosphatidylcholine/cholesterol unilamellar vesicles using valinomycin in conjunction with a potassium ion gradient; this potential is monitored using the externally added fluorescent dye Safranine O. In the same system, transmembrance calcium fluxes are then detected using the (internally trapped) fluorescent dye Quin-2. The calcium-transport behavior of the channel-forming peptide alamethicin is shown to be potential dependent in this system, in contrast to calcium transport by the ionophore Br-A23187, which is unaffected by the potential. The observation of this potential-dependent behavior for alamethicin suggests that this vesicle system may be suitable for direct spectroscopic observation of the voitage-gating process.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 8
    ISSN: 0006-3525
    Schlagwort(e): Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Transmembrane (TM) regions of receptor proteins should have unique structural and/or chemical characteristics if these regions contain residues functional in TM signal transduction. However, in a survey of the membrane-occurring residues in 37 integral membrane proteins, we found that amino acid compositions of TM regions of receptor proteins (n = 11) could not be distinguished statistically from corresponding regions of membrane-anchored proteins (e.g., recognition molecules) with a functional external domain attached to a single hydrophobic membrane-spanning anchor segment (n = 16). TM regions in both categories of proteins differed from the compositions of TM regions in membrane-transport proteins (n = 10). The analysis implies that TM regions in receptor proteins may function mainly to anchor (and position) receptors in their cellular membranes, and therefore residues in receptors that participate in signal transduction need not be restricted to these regions. In addition to mechanisms involving receptor aggregation, ligand-activated conformational perturbation of a receptor external aqueous domain, resulting in membrane penetration of hydrophobic segment(s) of this domain to produce intramembranous contact with its cytoplasmic domain, is hypothesized as a further possible mode of signal transduction.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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