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  • 1975-1979  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 288 (1978), S. 319-320 
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract An improvement of the ion source of the online fission product separator OSTIS allowed us to identify the new isotopes100Rb(50±10 msec),100Sr (170±80 msec) and148Cs(130±40 msec). Half-lives for99Rb(59±4 msec),99Sr(290±40 msec) and147Cs(235±10 msec) were redetermined. All values were obtained by following the activity build-up and decay with β-multiscaling and γ-multispectra measurements.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 290 (1979), S. 359-371 
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract A study of the beta decay of143Cs and143Ba fission products was undertaken by the use of two on-line mass-separators OSTIS and OSIRIS. Level schemes for143Ba and143La are deduced from gamma and conversion electron spectra,γ-γ andβ-γ coincidences.Q β values and ground state beta feedings were also measured. The nuclei143La and143Ba are tentatively inserted in a systematic of odd-even nuclei aroundA=143 and even-odd nuclei with 87 neutrons respectively.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The beta endpoint energies of the alkaline fission products88–94Rb and139–144Cs have been measured with an intrinsic Ge-detector at the OSTIS fission product separator. The linearity and high resolution of the detector yields an accuracy of up to a few keV. Additional beta gamma coincidence spectra allow the deduction of Qβ-values.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Half-lives and delayed-neutron emission probabilities (P n ) of short-lived Rb and Cs precursors in the mass chains 94–98 and 143–147 were measured. Sources of isotope separated nuclides were obtained from the on-line mass-separator OSTIS installed at the Grenoble high-flux reactor. A newP n -value of (25.4±3.2)% is given for the (214±30) ms147Cs; theP n -values of nine alkali precursor nuclides were redetermined: (2,730±20) ms94Rb with (9.7±0.5)%, (377 ±6)ms95Rb with (8.6±0.5)%, (197±5)ms96Rb with (12.5±0.9)%, (171±4) ms97Rb with (25.2±1.8)%, (114±13)ms98Rb with (18.4±2.9)%, (1,765±30)ms143Cs with (1.74 ±0.12)%, (1,000±10)ms144Cs with (2.95±0.25)%, (616±20) ms145Cs with (12.2±0.9)%, (325±10)ms146Cs with (13.2±0.8)%. The results are compared with the existing data, and theP n -values are discussed within some simple model predictions.
    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: The stepwise synthesis and conformational studies of the N-terminal helical partial sequence of the membrane-modifying polypeptide antibiotic alamethicin are described. The polyoxyethylen esters of the fragments N-t-Boc-L-Pro-Aib-Ala-Gln-Aib-Val-Aib-Gly-OH and N-Ac-Aib-L-Pro-Aib-Ala-Aib-Ala-Gln-Aib-Val-Aib-Gly-OH are synthesized using polyoxyethylene (molecular mass 10,000) as solubilizing support. CD spectra of each intermediate in ethanol show α-helix formation of the N-protected peptide polymers beginning with the nonapeptide and of the N-protonated sequences beginning with the decapeptide. Compared to the helix of alamethicin, temperature- and solvent-dependent CD measurements indicate analogous conformational behavior. The results suggest that in lipophilic media the alamethicin helix can extend the full length of the partial sequence between the two proline residues and that aqueous media favor an increase of random-coil conformation.For model studies of the particular lipid interaction of alamethicin, the stepwise synthesis of peptides with the alternating (Aib-L-Ala)n sequence (n = 1-7) was carried out on a polyoxyethylene support (molecular mass 6000). CD and ORD studies in ethanol showed a change from the random coil to a right-handed α-helix with increasing peptide length. This change is observed for the N-protected peptides at a chain length of 8 residues and for the N-protonated peptides at a length of 9 residues. The comparison of the CD data of free and polyoxyethylene-bound peptides revealed that the solubilizing polymeric support cannot induce conformational changes. The intensities of the CD bands of t-Boc-(Aib-L-Ala)n-OPOE (n ≥ 6) are higher than those of alamethicin, and these model peptides show similar temperature and solvent inducible changes of their helix contents.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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