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  • 1
    Electronic Resource
    Electronic Resource
    Opioid-binding protein (OBCAM) is rich in β-sheets (1990)
    Springer
    The protein journal 9 (1990), S. 3-7 
    Details
    ISSN: 1573-4943
    Keywords: Opioid-binding proteins ; conformation ; circular dichroism ; sequence-predictive method
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Based on circular dichroism (CD) and the sequence-predictive method, the opioid-binding cell adhesion molecule (OBCAM) consisted of one half β-sheets and one fourth α-helices. This is consistent with significant sequence homology of the protein to several members of the immunoglobulin (Ig) superfamily, particularly cell adhesion molecules, which are rich in β-sheets. Hydropathy analysis suggests that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH2- and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23–30 and 83–93 were amphiphathie β-sheets. The overall conformation of OBCAM was unaltered by adding linoleic acid, which is required for opioid ligand binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024977
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Conformation and activity ofPhaseolus coccineus var. rubronanus lectin (1993)
    Springer
    The protein journal 12 (1993), S. 153-157 
    Details
    ISSN: 1573-4943
    Keywords: Glycoprotein ; lectin ; circular dichroism ; hemagglutinating activity ; denaturation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The conformation of native and denaturedPhaseolus coccineus var. rubronanus lectin was studied by circular dichroism (CD) and correlated to the hemagglutinating activity. The far-UV CD spectrum at 25°C showed a broad, negative band around 223 nm and a positive one at 196 nm. CD data analysis of the lectin indicated a β-sheet-rich protein. At high temperatures, the spectrum was blue-shifted with increasing magnitude; these changes correlated well with the loss of the activity. The conformation of lectin betweenpH 2 and 10 remained essentially unchanged. AtpH 13 the CD spectrum resembled that of unordered form with a negative band near 200 nm and the activity was completely lost. The denatured lectin in 6 M guanidine hydrochloride would be renatured upon diluting the denaturant to 0.75 M; the changes in CD spectrum again correlated well with the loss of the activity. The effect of sodium dodecyl sulfate on the lectin was drastic; it sharply increased thea-helix at the expense of the β-sheet and reduced the activity; the changes reached a plateau above 20 mM surfactant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01026036
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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