Abstract
The optical activity of a protein solution is very sensitive to changes in the protein configuration. Thus, the large increase in levorotation that commonly occurs when a protein solution is heated has been interpreted as the result of a protein unfolding process. A detailed study of the effects of temperature and urea on the unfolding of ribonuclease and lysozyme has just been completed in this laboratory. (Foss and Schellman 1959, Foss, submitted for publication.) While the optical activity of a protein is a sensitive measure of configurational changes it gives no direct information about what amino acid residues are participating in the unfolding. This paper is a preliminary report on some spectral measurements which clearly implicate some of the side chain chromophores in the heat induced unfolding process.
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