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1983 (1)
1977 (1)
1Author    Hugo Scheer, W. Erner KuferRequires cookie*
 Title    Conformational Studies on C-Phycocyanin from Spirulina platensis  
 Abstract    The chromophore-protein interactions of C-phycocyanin (C-PC) from Spirulina platensis have been studied by following the partial and complete denaturation with UV-Vis spectroscopy. From comparison with published MO calculations, an elongated conformation of the chromophore is sug­ gested for native C-PC, a cyclic one for denatured C-PC. By means of partial denaturation, a step­ wise unfolding of the protein has been demonstrated. The presence of at least two sets of spectro­ scopically different diromophores is suggested from the partial denaturation and low temperature experiments. 
  Reference    (Z. Naturforsch. 32c, 513 [1977]; received April 25 1977) 
  Published    1977 
  Keywords    Bile Pigments, Protein Interaction, Conformation, Denaturation 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0513.pdf 
 Identifier    ZNC-1977-32c-0513 
 Volume    32 
2Author    C. Schamagl, E. Köst-Reyes, S. Schneider, H.-P Köst, H. ScheerRequires cookie*
 Title    Circular Dichroism of Chromopeptides from Phycocyanin  
 Abstract    The circular dichroism of bilipeptides from Spirulina geitleri phycocyanin is strongly solvent and pH dependent. Maximum optical activity has been observed in aqueous solutions containing urea (8 M). In aqueous buffer, a sign reversal occurred upon the change from neutral to acidic pH; in methanolic solutions shows the optical activity a strong pH dependence both with respect to sign and magnitude. These findings have been rationalized by the presence o f chrom ophore-peptide interactions, which are minim ized in the presence of urea. M olecular orbital calculations indicate that the observed sign reversal is not necessarily due to a reversal o f the chirality o f the entire chromophore, but may also result from more localized conform ational changes. 
  Reference    Z. Naturforsch. 38c, 951—959 (1983); received June 22 1983 
  Published    1983 
  Keywords    Biliproteins, Bilipeptides, Conform ation, Optical Activity, Protein Interaction 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0951.pdf 
 Identifier    ZNC-1983-38c-0951 
 Volume    38