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Glycine and Alanine

This article describes two basic amino acids: glycine (Gly) and alanine (Ala). This is mainly because they can be used as base amino acids, and adding groups to them can generate other kinds of amino acids.


Glycine has a special sweet taste, so its English name comes from the Greek word glykys (sweet). The Chinese translation of glycine not only means "sweet", but also has a similar pronunciation, which can be called a model of "faithfulness, expressiveness and elegance". Due to the sweetness of glycine, it is often used as a flavoring agent in the food industry to remove bitterness and increase sweetness. Glycine has a small side chain with only one hydrogen atom. This sets him apart. It is a basic amino acid without chirality.


Glycine is characterized by its small size and flexibility in proteins. For example, the triple helix conformation of collagen is very special. Every two residues must have a glycine, otherwise too much steric hindrance will result. Likewise, linkage between two domains of a protein often requires glycine to provide conformational flexibility. However, if glycine is sufficiently flexible, its stability must be insufficient.

Glycine is one of the disruptors during the formation of α-helices. The reason is that the side chain is too small and the conformation cannot be stabilized at all. Additionally, glycine is commonly used in the preparation of buffered solutions. People who often do electrophoresis experiments must remember.


The English name of alanine comes from the German acetaldehyde, and the Chinese name is easier to understand, because alanine contains three carbons, and the chemical name is aminopropionic acid. It's a simple name, like the character of an amino acid. Alanine has only one methyl group in its side chain, which is slightly larger than glycine. When I drew the structural formulas for the other 18 amino acids, I added groups to alanine. In proteins, alanine is like a brick, a common basic building material that does not conflict with anyone.


The alanine side chain has little steric hindrance and is located in the α-helix, which is a conformation; the β-sheet is also very stable. In protein engineering, if you want to mutate an amino acid on a protein that does not have a specific target, you can generally mutate it to alanine, which is not easy to destroy the overall conformation of the protein.