Abstract
A century ago it was first observed that amino acids underwent racemization when heated in strongly acidic and basic solutions. It soon became well established that the optically active amino acids isolated from biological materials could be converted into a racemic mixture by a variety of rather vigorous treatments. In the early part of the 20th century the first observations of amino acid racemization in peptides and proteins in alkaline solutions at elevated temperatures were reported. The interpretation of these measurements was complicated by peptide-bond hydrolysis and the realization that racemization rates probably depended on whether amino acids were at terminal or internal positions in the peptide. The earlier work on amino acid racemization in various systems was extensively reviewed in 1948 by Neuberger [1].
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