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In 1995, the same group reported structural characterization of a prototypical IDP, prothymosin α, using SLS and DLS in combination with SAXS, circular dichroism, and mass spectrometry, indicating that the protein is a biologically active protein with random coil conformation characterized by the shape factor of 1.55 and complete lack of ordered secondary structure and concluding: “The finding that a biologically active protein molecule with 109 amino acid residues adopts a random coil conformation under physiological conditions raises the question whether this is a rare or a hitherto-overlooked but widespread phenomenon in the field of macromolecular polypeptides” (Gast et al., 1995)

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