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1984 (1)
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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    Axel Ganzhom, Margrit Scharschm, G.Erhard PfleidererRequires cookie*
 Title    Über die pH-induzierte Inaktivierung der Glycerindehydrogenase aus Bacillus megaterium  
 Abstract    -Induced In activ atio n o f G ly cero l D e h y d ro g e n a s e from Bacillus m egaterium The kinetic o f the reversible dissociation o f glycerol dehydrogenase from Bacillus m egaterium in slightly alkaline medium was measured by biochem ical, chem ical and physical m ethods. The dissociation is followed by changes in the secondary structure and can be prevented by addition o f N A D or increased potassium chloride concentration. Crosslinking by suberim idate, but not by monofunctional im ido esters, shows a high stabilization against alkali, urea or heat inactivation caused by hindrance o f dissociation. 
  Reference    Z. Naturforsch. 39c, 575—583 (1984); received January 31 1984 
  Published    1984 
  Keywords    Dissociation, Reassociation, Glycerol Dehydrogenase, Crosslinking, Denaturation 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0575.pdf 
 Identifier    ZNC-1984-39c-0575 
 Volume    39 
3Author    MichaelS. Clegg, DieterW. GruenwedelRequires cookie*
 Title    Circular Dichroism and Ultraviolet Absorbance of Calf Thymus D NA in Presence of C H 3HgOH  
 Abstract    The changes that one observes upon the addition of CH3HgOH in the circular dichroism spec­ trum and ultraviolet absorbance spectrum of native calf thymus DNA, dissolved in buffered (pH 6.8) solutions of Na2S04 at pNa 2.0, 1.5, 1.0, and 0.0, respectively (p N a = —log [Na+ ]), are shown to be due to denaturation brought about by the organomercurial interacting with the base moieties of the polymer. The changes are characterized by an extensive shift of both spectra to longer wavelengths, by a decrease of the rotational strength of the long-wavelength positive dichroic absorption band, and by an increase in the UV absorbance at l max • Both the hyperchromicity H * of calf thymus DNA and the normalized decrease of the rotational strength of its long-wavelength positive dichromic band, Q , display cooperativity when plotted against the methylmercury concentra­ tion pM (p M = — log [CH3HgOH] a dde d) at a given salt strength. Rotational strength data, eval­ uated by integration of the area under the positive and negative dichroic absorption bands, have been tabulated for selected values of pNa and pM. They are compared with data available from the literature. In absence of CH3HgOH, and with varying salt strength, native calf thymus DNA exhibits alterations in the long-wavelength positive dichroic absorption band that are interpreted as representing B — * ■ C transitions in agreement with currently held views regarding their origin. Similar salt-induced alterations have been noted in the case of denatured DNA; their meaning in terms of DNA geometry remains unclear at this point in time. 
  Reference    Z. Naturforsch. 34c, 259—265 (1979); received November 27 1978 
  Published    1979 
  Keywords    Circular Dichroism, Ultraviolet Absorbance, Calf Thymus DNA, Methylmercury Complexes, Denaturation 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0259.pdf 
 Identifier    ZNC-1979-34c-0259 
 Volume    34 
4Author    Elisabeth Langer, H. Arald Lehner, Wolfhart Rüdiger, Barbara Zickendraht, -W EndelstadtRequires cookie*
 Title    Circular Dichroism of C-Phycoerythrin: A Conformational Analysis  
 Abstract    An extensive study o f the chiroptical properties o f C-phycoerythrin and the a-and ^-subunits in the spectral region from 700 -200 nm is presented. Based on the VIS-circular dichroism inherently chiral conform ations are proposed for the co­ valently linked chromophores. By means o f mean residue ellipticities and the experimental circular dichroism spectra in the region o f the n -* n* peptide transition the a-helix contents o f the apoproteins o f the ac-and ß-subunits are estimated to amount to 60% and 40%, respectively. The circular dichroism spectrum o f native C-phycoerythrin is congruent with a linear superposition o f the a-and /?-subspectra, in the whole spectral region studied. Since a-and /?-subunits are associated in native C-phycoery-thrin as revealed by sedim entation analysis the interactions between the subunits in the native chromoprotein are not accom panied by substantial conform ational changes. In the temperature range 0 ° -4 0 °C the thermally induced changes o f the chrom ophores in native C-phycoerythrin are not associated with changes o f the secondary structure o f the apoprotein. Unfolding occurs at 60 0 -7 0 °C but slowly leads to irreversible denaturation. Protein unfolding starts at 3 M urea. The random coil secondary structure o f the apoproteins is reached at 8 M urea. At this concentration the absorbance and the optical activity o f the chrom o­ phores are reduced by a factor 3 and 10, respectively. The conformational changes in the peptide with increasing denaturant concentration are not synchronous with those induced in the Chromo­ phore indicating that a m ultistep process is operative during unfolding. The C D results on dena­ turation are supplem ented by absorption and em ission spectroscopy. 
  Reference    Z. Naturforsch. 35c, 367 (1980); received February 5 1980 
  Published    1980 
  Keywords    Phycoerythrin, Subunits, Conformation o f Chrom ophores and Apoproteins, Circular D ichroism, Denaturation 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0367.pdf 
 Identifier    ZNC-1980-35c-0367 
 Volume    35