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  • 61.10  (1)
  • Caenorhabditis elegans  (1)
  • 1995-1999  (2)
  • 1
    ISSN: 1432-0630
    Keywords: 68.55 ; 61.10 ; 81.40.Ef
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The growth of epitaxial C60 thin films on mica(001) by thermal evaporation has been studied in detail by X-ray pole-figure measurements. The influence of the deposition rate, the substrate temperature and the film thickness on the in-plane epitaxial arrangements and the formation of twins has been investigated. It has been demonstrated that the C60 growth is determined by two independent and equivalent C60-crystal grain alignments (type-A and type-B). The nearly six-fold symmetry of the mica(001)-substrate surface offers the three-fold fcc-(111)-oriented C60-crystal grains two equivalent crystal alignments. A high deposition rate of 0.5 Å/s is responsible for the formation of twins at a substrate temperature of 150°C, which diminishes by a higher substrate temperature of 200°C. By a decrease of the deposition rate down to 0.08 Å/s the twins vanish at a film thickness of 200 nm and at the substrate temperature of 150°C. Under the same sublimation conditions, in addition to the type-A and type-B crystal orientations, the growth of the thin C60 films starts with a slight fibre texture which does not appear at a larger film thickness.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Caenorhabditis elegans ; Two-dimensional polyacrylamide gel electrophoresis ; Microsequencing ; Protein maps ; Immobilized pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Employing isoelectric focusing on immobilized pH gradients followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) we have obtained a map of C. elegans proteins, from a mixed culture containing all developmental stages, presenting over 2000 spots within the window of isoelectric points (pI) 3.5-9 and a molecular mass of 10-200 kDa. Edman microsequencing yielded successful results in 12 out of 24 analyzed spots. All but one of the N-terminal sequences retrieved C. elegans sequences in cosmid and/or expressed sequence tag clones. Structurally related protein sequences found in data banks included enzymes in energy metabolism (cytochrome oxydase, ATP synthase, enolase), a fatty acid-binding protein, a translationally controlled tumor protein, an unknown C. elegans protein, an acidic ribosomal protein, a titin-like protein, a G-protein β chain, cyclophilin, and cathepsin D. Experimental determination of N-termini allowed us to define sites of signal cleavage providing further information on the physiological role of the newly found C. elegans proteins. This report demonstrates the possibility of two-dimensional gel electrophoresis and Edman microsequencing in the elucidation of C. elegans proteome.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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