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  • American Association for the Advancement of Science (AAAS)  (3)
  • American Institute of Physics (AIP)  (3)
  • 2010-2014
  • 2000-2004  (6)
  • 1995-1999
  • 1960-1964
  • 2002  (6)
  • 1
    Digitale Medien
    Digitale Medien
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 91 (2002), S. 278-286 
    ISSN: 1089-7550
    Quelle: AIP Digital Archive
    Thema: Physik
    Notizen: Large angle picosecond reorientation of the magnetization has been studied in circular Ni81Fe19 thin-film elements of 30 μm diameter and 500 Å thickness by means of an optical pump–probe technique. The sample was pumped by an optically triggered magnetic field pulse and probed by a time resolved magneto-optical Kerr effect measurement. The temporal profile of the pulsed field and the in-plane uniaxial anisotropy of the element were first determined from measurements made in large static fields where the magnetization exhibited small amplitude ferromagnetic resonance oscillations. Measurements of large amplitude oscillations were then made in a smaller static field that was still larger than the in-plane uniaxial anisotropy field and sufficient to saturate the sample. Using the measured temporal profile of the pulsed field, the Landau–Lifshitz–Gilbert equation was used to model the motion of the magnetization as a coherent rotation process. The same values of the anisotropy and damping constants provided an adequate simulation of both the high and low field data. The magnetization was found to move through an angle of up to about 30° on subnanosecond time scales. The dependence of the reorientation upon the direction of the static applied field and observed deviations from the coherent precession model are discussed. © 2002 American Institute of Physics.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 80 (2002), S. 2032-2034 
    ISSN: 1077-3118
    Quelle: AIP Digital Archive
    Thema: Physik
    Notizen: Using a low-field magnetic resonance scanner, we have obtained images of gaseous polarized 129Xe and water cells at room temperature. This potentially low-cost imaging technique offers the possibility of high-resolution imaging using both polarized noble gas and proton magnetic resonance imaging of tissues in the same scanner. © 2002 American Institute of Physics.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    ISSN: 1089-7623
    Quelle: AIP Digital Archive
    Thema: Physik , Elektrotechnik, Elektronik, Nachrichtentechnik
    Notizen: We have constructed an apparatus for studying the infrared spectra of molecules with a doubly positive charge (molecular dications). The spectroscopic transitions were recorded indirectly by means of observing a change in the fragmentation rate of the molecular dication when a transition was in resonance. The design and performance of the spectrometer are described, with particular emphasis on the sensitivity achieved for detecting infrared spectra and Zeeman split infrared spectra. The operation and calibration of the spectrometer are discussed and sample results for DCl2+ are presented. It is shown that we achieve the maximum possible signal/noise ratio that could be achieved in this type of experiment. © 2002 American Institute of Physics.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Publikationsdatum: 2002-05-15
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baird, Andrew H -- Bellwood, David R -- Connell, Joseph H -- Cornell, Howard V -- Hughes, Terry P -- Karlson, Ronald H -- Rosen, Brian R -- New York, N.Y. -- Science. 2002 May 10;296(5570):1026-8; author reply 1026-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004903" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Climate ; *Cnidaria ; *Conservation of Natural Resources ; *Ecosystem ; Nephropidae ; Seawater ; Snails
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2002-05-07
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, Malcolm K -- New York, N.Y. -- Science. 2002 May 3;296(5569):848-9 author reply 848-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11989486" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Climate ; Temperature ; Time Factors ; Trees/growth & development/*physiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Publikationsdatum: 2002-04-06
    Beschreibung: The essential Cdc13 protein in the yeast Saccharomyces cerevisiae is a single-stranded telomeric DNA binding protein required for chromosome end protection and telomere replication. Here we report the solution structure of the Cdc13 DNA binding domain in complex with telomeric DNA. The structure reveals the use of a single OB (oligonucleotide/oligosaccharide binding) fold augmented by an unusually large loop for DNA recognition. This OB fold is structurally similar to OB folds found in the ciliated protozoan telomere end-binding protein, although no sequence similarity is apparent between them. The common usage of an OB fold for telomeric DNA interaction demonstrates conservation of end-protection mechanisms among eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitton-Fry, Rachel M -- Anderson, Emily M -- Hughes, Timothy R -- Lundblad, Victoria -- Wuttke, Deborah S -- GM55867/GM/NIGMS NIH HHS/ -- GM59414/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):145-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11935027" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; DNA, Fungal/chemistry/*metabolism ; DNA, Single-Stranded/chemistry/*metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Ligands ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism ; Telomere/*metabolism ; *Telomere-Binding Proteins
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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