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'Protein Conformations' in keywords
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1989 (1)
1987 (1)
1985 (1)
1Author    H. L. Casal, U. Köhler, H. H. Mantsch, F.M G Oñ, J.L R ArrondoRequires cookie*
 Title    Conformational Changes in Proteins Induced by Low Temperatures: an Infrared Study  
 Abstract    Infrared spectra of hemoglobin (met-hemoglobin) and myoglobin were recorded in the temperature range —110 °C to 30 °C. On cooling hydroalcoholic solutions of hemoglobin, the spectra indicate a conformational change (revealed by the appearance of a band at 1665 cm ') com­ patible with the appearance of distortions in its a-helical structure. In the case of myoglobin smaller effects are ob­ served. These conformational changes are entirely revers­ ible and do not occur in frozen aqueous solutions. 
  Reference    Z. Naturforsch. 42c, 1339—1342 (1987); received July 20/August 17 1987 
  Published    1987 
  Keywords    Hemoglobin, Myoglobin, Protein Conformation, FT-IR Cryobiology 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1339_n.pdf 
 Identifier    ZNC-1987-42c-1339_n 
 Volume    42 
2Author    R. Udolf Schendel, W. Olfhart, R. ÜdigerRequires cookie*
 Title    Electrophoresis and Electrofocusing of Phytochrome from Etiolated Avena sativa L  
 Abstract    Phytochrome from etiolated oat seedlings (Avena sativa L.) was investigated by "native" gel electrophoresis and by isoelectric focusing. At pH 8 . 8 the Pfr form migrated faster than the Pr form in electrophoresis. We assume a difference in the surface charge rather than a difference in shape for the phytochrome forms. This assumption was confirmed by isoelectric focusing which clearly showed relatively more negative charge in the Pfr form than in the Pr form. The role of the peptide region from residue 323 to 360 is discussed in this connection. It carries 9 negatively charged residues, it is exposed only in the Pfr form and it has already been described as a signal region for rapid protein degradation (PEST sequence, see Rogers et al., Science 234, 364—368, 1986). The experiments on electrofocusing revealed a microheterogeneity of phytochrome which was present in the native state as well as in the completely unfolded state. The most probable reason could be either posttranslational modification or genetic polymorphism of phytochrome in oat. 
  Reference    Z. Naturforsch. 44c, 12 (1989); received November 25 1988 
  Published    1989 
  Keywords    Microheterogeneity, Pest Sequence, Phytochrome Denaturation, Protein Conformation 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0012.pdf 
 Identifier    ZNC-1989-44c-0012 
 Volume    44 
3Author    Gianfranco Menestrina, Flavia PasqualiRequires cookie*
 Title    Effects of Carbohydrates on the Ion Conductance of the Hemocyanin Channel  
 Abstract    The effects o f glucose and sucrose on the ionic conductance properties o f the channel formed by Megathura crenulata hemocyanin in planar lipid bilayers have been studied using m em branes o f different compositions. It was found that glucose at high concentrations strongly affects the time constants o f the current relaxations observed in m em branes containing many channels after a step in the voltage clamp from ground to a positive value. At m uch lower concentrations both sucrose and glucose strengthened the binding o f Ba2+ to the protein, what in turn has the effect to shift the conductance voltage curve o f the pore towards negative potentials. The possible mechanism underlying these effects and the analogies with other studies on the interaction o f sugars and alcohols with proteins have been discussed. 
  Reference    Z. Naturforsch. 40c, 85—9 (1985); received October 25 1984 
  Published    1985 
  Keywords    Hemocyanin Channel, Planar Lipid Bilayer, Carbohydrates, D ivalen t Cations, Protein Conformations 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0085.pdf 
 Identifier    ZNC-1985-40c-0085 
 Volume    40