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  • Alzheimer's disease  (1)
  • Calmodulin  (1)
  • Calmodulin fragments  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles (1992)
    Springer
    European biophysics journal 21 (1992), S. 345-348 
    Details
    ISSN: 1432-1017
    Keywords: Alzheimer's disease ; Amyloid A4 ; Conformational change ; Octyl glucoside
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The secondary structure of a synthetic amyloid fragment des [Ala21,30]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl β-d-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of a-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a β-sheet conformation. Secondary structure analysis yields a predominant (〉 70 %) β-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21,30]A42 interact with the sugar-coated surface of micelles, which promotes an a to β conformational transition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00188347
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Comparative analysis of the amino- and carboxy-terminal domains of calmodulin by Fourier transform infrared spectroscopy (1996)
    Springer
    European biophysics journal 24 (1996), S. 195-201 
    Details
    ISSN: 1432-1017
    Keywords: Calmodulin ; Calmodulin fragments ; FTIR spectroscopy ; Ca2+-binding effects
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Fourier transform infrared spectra were obtained for mammalian calmodulin and two of its fragments produced by limited proteolysis with trypsin TR1C (1–77) and TR2C (78–148). Experiments were done in H2O, D2O and D2O/trifluoroethanol (TFE) mixtures. Information about secondary structure was obtained from analysis of the amide I and II bands; while characteristic absorbances for tyrosine, phenylalanine and carboxylate groups were analyzed for changes in tertiary structure. Our data indicate that the secondary and tertiary structure is preserved in the two half molecules of CaM, both in the apo- and Ca2+-saturated state. Addition of the structure-inducing solvent TFE causes marked changes only in the apo-TR1C domain. The maximum wavenumber for the amide I band of the two domains of CaM in D20 was markedly different (1642 cm−1 for TR1C versus 1646/1648 cm−1 for Ca 2+ and apo-TR2C). This renders the amide I band for the intact protein very broad in comparison to that in other proteins and is indicative of a distribution of α-helices with slightly different hydrogen bonding patterns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00205100
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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