MadSci Network: Biochemistry |
Chai, To first understand how amino acids and proteins function as buffers in the body, you need to understand a little about the structure of an amino acid. If we look at the general structure of an amino acid, you can see that it has an amine (NH3) group on one end and a carboxyl (COOH) group on the other end. Example: glycine 3HN--CH2--COOH If the amino acid is in solution, as the pH changes the amino and carboxy hyrogens (protons) will be affected. using glycine as an example again: LOW pH NEUTRAL pH HIGH pH +3HN--CH2--COOH -> +3HN--CH2--COO- -> 2HN--CH2--COO +1 net charge neutral charge -1 net charge pH 2.3 pH 9.7 As you can see, as the pH changes a hydrogen can be lost or gained affecting the charge. Glycine is a simple example since it doesn't have any R groups attached to the carbon. Many R groups can also gain or lose hydrogens, such as arginine, glutamic acid, ect. This means that at any particular pH an amino acid may have a net + or - charge. To complicate this a little bit more, proteins are made up of many amino acids each of which contributes to the proteins overall charge. Remember that there will be only 1 terminal amine and carboxy group, BUT there will be many R groups affecting the charge. We now consider a basic definition of a buffer as a solution that consists of a mixture of a weak acid and it conjugate base. A good buffer will tend to resist changes in pH upon addition of moderate amounts of strong acid or base. Amino acids that have this capability are glycine and histidine. For proteins to act as buffers, you must take into account all of the R groups and the pH that they will gain or lose protons. To investigate this further, I suggest that you obtain a general chemistry and biochemistry textbook. I would especially recommend readings on hemoglobin and bisphosphoglycerate. Jeff Stiefel
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