Abstract
An important problem in the study of individual ribosomal proteins is to obtain information concerning their tertiary structure in solution. One method to show the existence of a tertiary structure in proteins is to study the disruption of the structure during the process of heat denaturation, using scanning microcalorimetry [ 11. This technique reveals conformational transitions of the ‘order-disorder’ type which are displayed as heat absorption peaks, their presence being a direct indication of the existence of a tertiary structure in the proteins under investigation [2]. Here a microcalorimetry study of isolated ribosomal
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