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Infrared spectra of hemoglobin (met-hemoglobin) and myoglobin were recorded in the temperature range -110 degrees C to 30 degrees C. On cooling hydroalcoholic solutions of hemoglobin, the spectra indicate a conformational change (revealed by the appearance of a band at 1665 cm-1) compatible with the appearance of distortions in its alpha-helical structure. In the case of myoglobin smaller effects are observed. These conformational changes are entirely reversible and do not occur in frozen aqueous solutions.
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Casal et al. (1987) studied this question.
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