Soluble proteins are essentially polypeptide chains arranged in unique but specific conformations. This form of organization is important for a wide range of biological activities, such as the transport of fatty acids and oxygen in blood serum albumin.
They are also important for regulating osmotic pressure in cells and for transporting amino acids to other proteins or organelles. They are a major class of protein molecules found in the cellular environment.
These proteins are generally globular in nature and are soluble in aqueous media. A notable example of a globular protein is hemoglobin, which binds oxygen. Other globular proteins include the a-lactalbumins, which are a large family of proteins that are responsible for transporting fatty acids and maintaining proper osmotic pressure in the body.
Solubility of a protein can be affected by a variety of intrinsic factors, including protein-protein interaction, surface polarity, and the presence of a precipitant. Despite the fact that many precipitants have been used to measure protein solubility, a comprehensive understanding of how these intrinsic factors influence solubility is still limited. Therefore, a comparative study of two representative proteins was performed using ammonium sulfate and polyethylene glycol 8000 to identify the parameters that contribute most to protein solubility in these precipitants.
