The authors of the article: Professor Mehdi Aria, professor of biology at the Oklahoma City Community College of United States

Proteins are one of the most fundamental biological macromolecules. Many are unstable when not in their native environment. Protein stability largely depends on the hydrophobic effects and static electricity interactions in the molecule. The structure of the protein is flexible and it is possible to have unpacked parts in the molecule. The denatured protein may reshape again under certain specific conditions. The stability and structure of the protein depends on the existance of an infinitely delicate balance between strong and neutralizing forces which makes the stability of the proteins very fragile. The energy value is, on average, 5.4 kj per mole. The stability depends on a number of factors. Intramolecular forces such as chemical bonds, charge-charge interactions, etc. and intermolecular interactions such as solvent effects, pH changes, etc. Most sustainability tests are carried out with complete sedimentation of proteins, which can indicate the required amount of bentonite needed to prevent protein instability.