Question: What number of standard amino acids exist?
About the article "Biochemistry", section "Proteins".

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In α amino acids (molecule at left), both the carboxylic acid group (red) and the amino group (blue) are bonded to the same carbon center, termed the α carbon (formula_1) because it is one atom away from the carboxylate group.
In β amino acids, the amino group is bonded to the β carbon (formula_2), which is found in most of the 20 standard amino acids.
Only glycine lacks a β carbon, which means that β-glycine is not possible.
The chemical synthesis of β amino acids can be challenging, especially given the diversity of functional groups bonded to the β carbon and the necessity of maintaining chirality.
In the alanine molecule shown, the β carbon is achiral; however, most larger amino acids have a chiral formula_2 atom.
A number of synthesis mechanisms have been introduced to efficiently form β amino acids and their derivatives notably those based on the Arndt-Eistert synthesis.
Two main types of β-peptides exist: those with the organic residue (R) next to the amine are called β3-peptides and those with position next to the carbonyl group are called β2-peptides. 
The following illustrates the structures and abbreviations of the 21 amino acids that are directly encoded for protein synthesis by the genetic code of eukaryotes.
The structures given below are standard chemical structures, not the typical zwitterion forms that exist in aqueous solutions.IUPAC/IUBMB now also recommends standard abbreviations for the following two amino acids: 
Some non-α amino acids exist in organisms, such as β-alanine, GABA and δ-Aminolevulinic acid.
The reason why α amino acids are using in protein has been attributed to their frequency in meteorites and prebiotic experiments.
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An initial speculation on the deleterious properties of β amino acids in terms of secondary structure, turned out to be incorrect.
Additionally, several man-made inhibitors exist that are not α amino acids, such as isoserine. 
In meteorites and in prebiotic experiments (e.g.
Miller–Urey experiment) many more amino acids than the twenty standard amino acids are found, several of which at higher concentrations that the standard ones: it has been conjectured that if amino acid based life were to arise in parallel elsewhere in the universe, no more than 75% of the amino acids would be in common.
The most notable anomaly is the lack of aminobutyric acid. 
Like carbohydrates, some proteins perform largely structural roles.
For instance, movements of the proteins actin and myosin ultimately are responsible for the contraction of skeletal muscle.
One property many proteins have is that they specifically bind to a certain molecule or class of molecules—they may be "extremely" selective in what they bind.
Antibodies are an example of proteins that attach to one specific type of molecule.
In fact, the enzyme-linked immunosorbent assay (ELISA), which uses antibodies, is one of the most sensitive tests modern medicine uses to detect various biomolecules.
Probably the most important proteins, however, are the enzymes.
These molecules recognize specific reactant molecules called "substrates"; they then catalyze the reaction between them.
By lowering the activation energy, the enzyme speeds up that reaction by a rate of 1011 or more: a reaction that would normally take over 3,000 years to complete spontaneously might take less than a second with an enzyme.
The enzyme itself is not used up in the process, and is free to catalyze the same reaction with a new set of substrates.
Using various modifiers, the activity of the enzyme can be regulated, enabling control of the biochemistry of the cell as a whole.
In essence, proteins are chains of amino acids.
An amino acid consists of a carbon atom bound to four groups.
One is an amino group, —NH2, and one is a carboxylic acid group, —COOH (although these exist as —NH3+ and —COO− under physiologic conditions).
The third is a simple hydrogen atom.
The fourth is commonly denoted "—R" and is different for each amino acid.
There are 20 standard amino acids.
Some of these have functions by themselves or in a modified form; for instance, glutamate functions as an important neurotransmitter.
Amino acids can be joined via a peptide bond.
In this dehydration synthesis, a water molecule is removed and the peptide bond connects the nitrogen of one amino acid's amino group to the carbon of the other's carboxylic acid group.
The resulting molecule is called a "dipeptide", and short stretches of amino acids (usually, fewer than thirty) are called "peptides" or polypeptides.
Longer stretches merit the title "proteins".
As an example, the important blood serum protein albumin contains 585 amino acid residues.
The structure of proteins is traditionally described in a hierarchy of four levels.
The primary structure of a protein simply consists of its linear sequence of amino acids; for instance, "alanine-glycine-tryptophan-serine-glutamate-asparagine-glycine-lysine-…".
Secondary structure is concerned with local morphology (morphology being the study of structure).
Some combinations of amino acids will tend to curl up in a coil called an α-helix or into a sheet called a β-sheet; some α-helixes can be seen in the hemoglobin schematic above.
Tertiary structure is the entire three-dimensional shape of the protein.
This shape is determined by the sequence of amino acids.
In fact, a single change can change the entire structure.
The alpha chain of hemoglobin contains 146 amino acid residues; substitution of the glutamate residue at position 6 with a valine residue changes the behavior of hemoglobin so much that it results in sickle-cell disease.
Finally, quaternary structure is concerned with the structure of a protein with multiple peptide subunits, like hemoglobin with its four subunits.
Not all proteins have more than one subunit.
Ingested proteins are usually broken up into single amino acids or dipeptides in the small intestine, and then absorbed.
They can then be joined to make new proteins.
Intermediate products of glycolysis, the citric acid cycle, and the pentose phosphate pathway can be used to make all twenty amino acids, and most bacteria and plants possess all the necessary enzymes to synthesize them.
Humans and other mammals, however, can synthesize only half of them.
They cannot synthesize isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.
These are the essential amino acids, since it is essential to ingest them.
Mammals do possess the enzymes to synthesize alanine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, proline, serine, and tyrosine, the nonessential amino acids.
While they can synthesize arginine and histidine, they cannot produce it in sufficient amounts for young, growing animals, and so these are often considered essential amino acids.
If the amino group is removed from an amino acid, it leaves behind a carbon skeleton called an α-keto acid.
Enzymes called transaminases can easily transfer the amino group from one amino acid (making it an α-keto acid) to another α-keto acid (making it an amino acid).
This is important in the biosynthesis of amino acids, as for many of the pathways, intermediates from other biochemical pathways are converted to the α-keto acid skeleton, and then an amino group is added, often via transamination.
The amino acids may then be linked together to make a protein.
A similar process is used to break down proteins.
It is first hydrolyzed into its component amino acids.
Free ammonia (NH3), existing as the ammonium ion (NH4+) in blood, is toxic to life forms.
A suitable method for excreting it must therefore exist.
Different tactics have evolved in different animals, depending on the animals' needs.
Unicellular organisms, of course, simply release the ammonia into the environment.
Likewise, bony fish can release the ammonia into the water where it is quickly diluted.
In general, mammals convert the ammonia into urea, via the urea cycle.