Protein Solubility

Protein Solubility 3351
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At the surfaces of proteins are amino acid residues that interact with water. The amino acids are referred to as hydrophilic amino acids and include arginine, lysine, aspartic acid, and glutamic acid. At pH 7 the side chains of these amino acids carry charges—positive for arginine and lysine, negative

A scientist adjusts equipment used in fast protein liquid chromatography, which is used to isolate specific proteins from sample mixtures. Soluble proteins have a charge on their surfaces.
A scientist adjusts equipment used in fast protein liquid chromatography, which is used to isolate specific proteins from sample mixtures. Soluble proteins have a charge on their surfaces.

for aspartic acid and glutamic acid. As the pH increases, lysine and arginine begin to lose their positive charge, and at pHs greater than about 12 they are mainly neutral. In contrast, as pH decreases, aspartic acid and glutamic acid begin to lose their negative charges, and at pHs less than 4 they are mainly neutral.

The surface of a protein has a net charge that depends on the number and identities of the charged amino acids, and on pH. At a specific pH the positive and negative charges will balance and the net charge will be zero. This pH is called the isoelectric point, and for most proteins it occurs in the pH range of 5.5 to 8. A protein has its lowest solubility at its isoelectric point. If there is a charge at the protein surface, the protein prefers to interact with water, rather than with other protein molecules. This charge makes it more soluble. Without a net charge, protein-protein interactions and precipitation are more likely.

The solubility of proteins in blood requires a pH in the range of 7.35 to 7.45. The bicarbonate–carbonic acid buffer system of blood (HCO 3 + H + ↔ H 2 CO 3 ), in which the bicarbonate is in excess of the carbonic acid, helps to maintain the correct pH. Exhalation of carbon dioxide from the lungs causes some of the bicarbonate ions in blood to combine with protons, and this would raise the pH. However, because there is an excess of bicarbonate ions and protons, the loss of a small number of protons does not influence the pH significantly.

The proteins of protein mixtures can be separated using a technique known as isoelectric focusing. A mixture is placed in a polyacrylamide gel that has a pH gradient. An anode (positive electrode) and a cathode (negative electrode) are positioned at the low and high ends of the pH gradient, respectively. If a protein is located in the high pH region, it will be negatively charged and will move toward the anode. As the protein moves to a lower pH region, its surface charge will become less negative, and a pH region will be reached at which the protein net charge is zero (the isoelectric point). The protein will stop moving and, because different proteins have different isoelectric points, separation can be achieved.

SEE ALSO Proteins .

Ian S. Haworth


Alberts, Bruce; Bray, Dennis; Johnson, Alexander; et al. (1998). Essential Cell Biology: An Introduction to the Molecular Biology of the Cell. New York: Garland.

Internet Resources

"Proteins." Unilever Education Advanced Series. Available from .

User Contributions:

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Aug 11, 2009 @ 2:14 pm
I am separating the proteins with charged magnetic particles , So on what pH i can separate cationic and anionic proteins by using opposite charged magnetic particles.
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Mar 29, 2011 @ 6:18 pm
What is protein solubility? In what ways does protein solubility vary with the pH? Effects of protein solubility on pH.
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Aug 1, 2012 @ 5:05 am
Good day Sir,
How does pH affect protein solubility or what are the effects of pH on protein solubility? I'm having some results conflicting with literature here.Please help!
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Nov 8, 2012 @ 8:08 am
why protein hydrolysis leads to an increase in viscosity?
patrick kimuyu
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Mar 15, 2013 @ 3:03 am
Transport proteins such as albumin and hemoglobin are structurally different from other functional proteins; how can they be precipitated on the basis of PH?

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