Springer Online Journal Archives 1860-2000
Chemistry and Pharmacology
Abstract Infrared spectra of several globular proteins have been recorded in fluid solutions (hydro-alcoholic mixtures) in the temperature range −110° C to 30° C. In the case of hemoglobin, which has a highly ordered secondary structure, smaller spectral changes are observed which are compatible with distortions of itsα helices. In contrast to this,β-casein, a protein with mostly unordered structure, undergoes a much larger change whereby low temperature induces folding of the protein chains.
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