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In 1995, the same group reported structural characterization of a prototypical IDP, prothymosin , 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)

The main difference lies in their primary research focus

Ther Adv Med Oncol

Pernicious anemia occurs when the body lacks intrinsic factor, a protein needed to absorb vitamin B12 from food