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In fact, in 1958, he reported the results of the analysis of a highly phosphorylated protein from egg yolk, phosvitin (curiously, with more than 90% of its serine amino acids being phosphorylated and with 10% phosphorus content, phosvitin is considered as the most phosphorylated protein in nature (Yilmaz and Agagunduz, 2020)), by viscometry and ORD, and suggested that this protein is characterized by a flexible, disordered structure, which is similar to that of disordered polyglutamate (Jirgensons, 1958)