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  • Polymer and Materials Science  (4)
  • Insertional mutagenesis  (1)
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  • 1
    ISSN: 1618-0860
    Keywords: Bsr-REMI ; Dictyostelium discoideum ; Insertional mutagenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using a plasmid pBsr2 which carries a blasticidin S-resistant gene, we have improved the method of REMI (restriction enzyme-mediated integration) provided for insertional mutagenesis inDictyostelium discoideum (bsr-REMI). To confirm usefulness of thebsr-REMI, transformation efficiency, copy number of integrated DNA, and randomness of integration into genome were examined.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Measurements of the molecular weight of (Pro-Pro-Gly)n and (Pro-Pro-Gly)n(Ala-Pro-Gly)m(Pro-Pro-Gly)n, which were synthesized by the solid-phase method, revealed that they formed a trimer in an aqueous solution, and dissociated into single-stranded chains on warming. Accompanying the transition, a large decrease of optical rotation was observed, like the collagen-gelatin transition. The shape of the trimeric molecule was rodlike, and the dimensions were 12 Å in diameter and 2.8 Å per residue in length, regardless of the length of Ala-Pro-Gly sequences in a peptide chain. The data indicate that both Pro-Pro-Gly sequences and Ala-Pro-Gly sequences from the triple-helical structure similar to that of collagen in aqueous solution. All optical rotational dispersion (ORD) curves of solutions of the peptides were represented by a single-term Drude equation, and the Drude constant λc was 200 nm for all peptides regardless of the length of Ala-Pro-Gly sequences. The resemblance between the helical structure formed by Pro-Pro-Gly sequences and that by Ala-Pro-Gly sequences was also suggested by the formation of the hybrid triple helix from two kinds of peptide chains with different lengths of Ala-Pro-Gly sequences.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 13 (1974), S. 2385-2390 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: As model peptides of collagen, (Pro-Pro-Gly)n (n = 10, 12, 14, and 15) and (Pro-Pro-Gly)n(Ala-Pro-Gly)m(Pro-Pro-Gly)n (2n + m = 15; m = 1, 3, and 5) were synthesized by the solid-phase method. The final products were pure when checked by high-voltage paper electrophoresis and by amino acid analysis. Elemental composition was also examined.
    Additional Material: 1 Tab.
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 13 (1974), S. 2461-2475 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The analysis of thermal melting curves of (PPG)n (n = 10, 12, 14, and 15) and (PPG)n(APG)m (PPG)n (2n + m = 15; m = 1, 3, and 5) revealed that the enthalpy and entropy changes accompanying the transition from the random coil to the triple helix are -2500 cal and -6.3 e.u. per one mole of the tripeptide of the form of Pro-Pro-Gly, and -3100 cal and -11.2 e.u. per one mole of the tripeptide of the form of Ala-Pro-Gly.The thermal instability of the triple helix composed of Ala-Pro-Gly sequences, compared to the helix of Pro-Pro-Gly sequences, is due to the larger entropy change of Ala-Pro-Gly (-11.2 e.u.) compared to that of Pro-Pro-Gly (-6.3 e.u.), not from the difference in the enthalpy change.The difference in the enthalpy change between Pro-Pro-Gly and Ala-Pro-Gly arises from the hydrophobic bond between two pyrrolidine rings of proline residues formed in the triple helix. Since the enthalpy change for the formation of hydrophobic bonds is positive, it is also concluded that only one hydrogen bond is formed in a tripeptide unit, regardless of the amino acid sequence. The enthalpy change for the formation of this hydrogen bond is -3100 cal/mol, and that of the hydrophobic bond between two pyrrolidine rings is +600 cal/mol.
    Additional Material: 6 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 13 (1974), S. 2477-2488 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The kinetic curves of the helix-refolding of (PPG)n (n = 10, 12, and 15) were analyzed with an all-or-none model. The Arrhenius plot of the overall rate constant of the helixfolding kF showed a negative activation energy at high temperature. With the aid of a sequential model, it was concluded that the reason for the anomaly was the instability of short helices (shorter than seven helical units in a trimeric molecule), and/or the more rapid rates of helix-folding and helix-opening for shorter helices.The rate constant of the formation of one helical unit composed of three tripeptides at an end of a long helix was calculated to be 102-4 sec-1. It was much smaller than that for other kinds of helices, such as an α helix (1010 sec-1) or a double helix of nucleic acids (107-9sec-1).
    Additional Material: 5 Ill.
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