Abstract
The pH-dependent conformational change of a type K Bence Jones protein (Ta) was studied by circular dichroism (CD)* * * * and ultraviolet spectroscopy. The conformation of this protein was stable between pH4 and 10 and was changed as the pH was lowered below pH4 or raised above 10. From the total change of the molar extinction coefficient upon acid denaturation it was suggested that two tryptophyl residues of Ta protein are exposed by the denaturation. CD spectra showed that the acid-denatured Ta protein is not randomly coiled but assumes some ordered structure, although the alkali-denatured protein is nearly randomly coiled.
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