In determining their composition, they were told they are polypetides formed into sphercal shapes which were mostly soluble in water. they concluded that these antibodies were globular protiens.
The term "globular protein" is fairly old (dating likely from the 19th century) and is now somewhat obsolete given the hundreds of thousands of proteins and more sophisticated and descriptive structural motif vocabulary. Only by using ultracentrifuges or dynamic light scattering techniques can the globular nature of these proteins be identified without the use of contemporary methods.
By virtue of the protein's tertiary structure, the spherical structure is induced. Apolar (hydrophobic) amino acids are bonded inside the molecule, whereas polar (hydrophilic) amino acids are bound outside. This allows for dipole-dipole interactions with the solvent, which explains why the molecule is soluble.
The free energy released when a protein folds into its native shape is relatively low, which makes globular proteins only weakly stable.
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