In 1943, 10 years after leaving Germany as a refugee, Albert Neuberger published two papers in the Biochemical Journal which became citation classics of their time. They concerned very different aspects of amino acid biochemistry. One, co-authored with John Crammer, described the discovery that the reactivity of the tyrosine side chains in ovalbumin differed considerably from that observed with the free amino acid, but changed substantially when ovalbumin was denatured. This provided some of the earliest evidence that the folded structure of proteins involves interactions between amino acid side chains. The other, with Fred Sanger, focused on the utility of different lysine derivatives as components of the diet. This extended Sanger and Neuberger's previous investigations into the nutritional value of the potato as a source of nitrogen, a line of work that they had initiated in response to the need to carry out research of greater relevance to the war effort. In the present article, I describe these two citation classics and place them in the context of my father's establishment of his career in the UK.

This content is only available as a PDF.