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1987 (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