| 1 | Author | H. L. Casal, U. Köhler, H. H. Mantsch, F.M G Oñ, J.L R Arrondo | Requires 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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