Amino Acids

Amino acids are a crucial, yet basic unit of protein, and they contain an amino group and a carboxylic
group. They play an extensive role in gene expression processes, which includes the adjustment of
protein functions that facilitate messenger RNA (mRNA) translation (Scot et al., 2006).

In nature, over 700 types of amino acids have been uncovered. Almost all of them are α-amino acids.
They have been discovered in: bacteria; fungi; algae; various other plants.

These amino acids are present in bigger molecules as:

• Essential components of peptides and proteins

• Basic structures

- Amines

• Other types of amide

• Acidic structures

- Carboxylic acids; phenols

• Esterified structures

- Ethyl acetate is an example of an ester, as is ethyl ethanoate.

- When carboxylic acids and alcohols are combined, they create an esterified structure, and they lose a
molecule of water during when combining.

- The hydrogen on the carboxyl group of acetic acid is replaced with an ethyl group.

• Alkylated structures

- Non-polar side chains (alkyl groups)

- Polar (amides, alcohol - depending on how many side chains they have)

- Leucine is an example of an alkylated structure.

Amino acids also exist in free form. In particular, 20 very important amino acids are crucial for life as
they contain peptides and proteins and are known to be the building blocks for all living things. They are
contained in living cells where they are used for protein synthesis. These amino acids are controlled by
genetics. But not all natural amino acids reside here. In fact, some very unusual amino acids are
contained in plant seeds, where they are not crucial to the mature plant. However, they ward off
predators and such for protection, giving off toxins or other unpleasant characteristics in order to help
certain plant species survive.

As mentioned above, amino acids are imperative for sustaining the health of the human body. They
largely promote the:

• Production of hormones

• Structure of muscles

• Human nervous system's healthy functioning

• Health of vital organs

• Normal cellular structure

If amino acids are deficient, then protein synthesis does not occur.

In addition to other positive body functions and growth, without alpha-amino acids, a person may
experience fatigue, irritability, hormonal imbalances, and sometimes even depression.

To understand the abbreviations of amino acids, it is important to know why they have been
abbreviated in the first place. This is to make them easy to identify and to shorten them in more
manageable three-letter systems. Here we'll take a look at the simplest amino acid, glycine. It is
depicted as H-Gly-OH, with the «H» and the «OH» being «H2O», which represents the H2O at the time
of amino acid condensing in order to form a peptide.

Gly-Gly

Another way to look at the three-letter abbreviation system is that it captures the amino acid residual
state, which comprises proteins and peptides. When this system was introduced, it was done so
primarily to save space, rather than simplify amino acid names. It is important to know that, when a
one-letter system is used, such as «G» for glycine, which is more commonly used nowadays, it is
referring to synthesized peptides from the coded amino acids groups. However, this one-letter system is
not to be referenced in other contexts.

How Amino Acids were Discovered

For the sake of a reference point, whether assumed or not, the amino acids we are focusing on here
have resulted from protein hydrolysis. So throughout the centuries and the years, amino acids have
been discovered in a variety of ways, though primarily by way of chemists and biochemists of high
intelligence who possessed the greatest of skills and patience, and who were innovative and creative in
their work.
Whether amino acid discoveries occurred due to chance, due to discipline and well-constructed
hypotheses, or due to those who applied new methods or reagents, only those considered the prime
scientific minds that were involved in discovering amino acids.

Protein chemistries and the study of them are age-old, with some dating back thousands of years ago.
Processes and technical applications such as glue preparation, cheese manufacturing, and even the
discovery of ammonia via the filtering, of dung or horn, occurred centuries ago. Moving forward in time
to 1820, Braconnot prepared glycine directly from gelatin. He was attempting to uncover whether
proteins acted like starch; they are decomposed acids with sugar production.

While progress was slow at that time, it has since gained plenty of speed, although the complicated
processes of protein composition have not entirely been uncovered even to this day. But many years
have gone by since Braconnot first initiated such observations.

In looking to the future, much more needs to be discovered about the analysis of amino acids, including
finding new amino acids. The theory of protein constitution has a ways to go in the field of biochemistry.
Once that is accomplished - but only until then will our knowledge of amino acids and proteins be
satiated. Yet it is likely that day will not come anytime soon. This all adds to the mystery, complexities,
and strong scientific value of amino acids.

Classifications of Amino Acids

Experts classify amino acids based on a variety of features, including whether people can acquire them
through diet. Accordingly, scientists recognize three amino acid types:

1. Nonessential

2. Essential

3. Conditionally essential

However, the classification as essential or nonessential does not actually reflect their importance, as all
20 amino acids are necessary for human health.

Eight of these amino acids are essential (or indispensable) and cannot be produced by the body. They
are:

• Leucine

• Isoleucine

• Lysine

• Threonine

• Methionine
• Phenylalanine

• Valine

• Tryptophan

Histidine is an amino acid that is categorized as semi-essential since the human body doesn't always
need it to properly function; therefore, dietary sources of it are not always essential. Meanwhile,
conditionally essential amino acids aren't usually required in the human diet, but do become essential
under certain circumstances.

Finally, nonessential amino acids are produced by the human body either from essential amino acids or
from normal protein breakdowns. Nonessential amino acids include:

• Asparagine

• Alanine

• Arginine

• Aspartic acid

• Cysteine

• Glutamic acid

• Glutamine

• Proline

• Glycine

• Tyrosine

• Serine

An additional amino acids' classification depends upon the side chain structure, and experts recognize
these five as:

• Cysteine and Methionine (amino acids containing sulfur)

• Asparagine, Serine, Threonine, and Glutamine (neutral amino acids)

• Glutamic acid and Aspartic acid (acidic); and Arginine and Lysine (basic)

• Leucine, Isoleucine, Glycine, Valine, and Alanine (aliphatic amino acids)

• Phenylalanine, Tryptophan, and Tyrosine (aromatic amino acids)

One final amino acid classification is categorized by the side chain structure that divides the list of 20
amino acids into four groups - two of which are the main groups and two that are subgroups. They are:

1. Non-polar

2. Polar

3. Acidic and polar

4. Basic and polar

For example, side chains having pure hydrocarbon alkyl or aromatic groups are considered non-polar,
and these amino acids are comprised of Phenylalanine, Glycine, Valine, Leucine, Alanine, Isoleucine,
Proline, Methionine, and Tryptophan. Meanwhile, if the side chain contains different polar groups like
amides, acids, and alcohols, they are classified as polar. Their list includes Tyrosine, Serine, Asparagine,
Threonine, Glutamine, and Cysteine. If the side chain contains a carboxylic acid, the amino acids in the
acidic-polar classification are Aspartic Acid and Glutamic Acid. Furthermore, if the side chain consists of
a carboxylic acid and basic-polar, these amino acids are Lysine, Arginine, and Histidine.

Properties of Amino Acids

Amino acid structure

The properties of α-amino acids are complex, yet simplistic in that every molecule of an amino acid
involves two functional groups: carboxyl (-COOH) and amino (-NH2).

As well, each molecule contains a side chain or an R group. And while alanine is an example of a
standard amino acid (which is used in the biosynthesis of proteins), each R group has very different
properties and functions.

Table of common amino acid abbreviations and properties

Name Three letter code One letter code Molecular

Weight Molecular

Formula Residue

Formula Residue Weight

(-H2O) pKa pKb pKx pl

Alanine Ala A 89.10 C3H7NO2 C3H5NO 71.08 2.34 9.69 – 6.00

Arginine Arg R 174.20 C6H14N4O2 C6H12N4O 156.19 2.17 9.04 12.48

10.76
Asparagine Asn N 132.12 C4H8N2O3 C4H6N2O2 114.11 2.02 8.80 –
5.41

Aspartic acid Asp D 133.11 C4H7NO4 C4H5NO3 115.09 1.88 9.60 3.65
2.77

Cysteine Cys C 121.16 C3H7NO2S C3H5NOS 103.15 1.96 10.28 8.18

5.07

Glutamic acid Glu E 147.13 C5H9NO4 C5H7NO3 129.12 2.19 9.67 4.25
3.22

Glutamine Gln Q 146.15 C5H10N2O3 C5H8N2O2 128.13 2.17 9.13 –

5.65

Glycine Gly G 75.07 C2H5NO2 C2H3NO 57.05 2.34 9.60 – 5.97

Histidine His H 155.16 C6H9N3O2 C6H7N3O 137.14 1.82 9.17 6.00

7.59

Hydroxyproline Hyp O 131.13 C5H9NO3 C5H7NO2 113.11 1.82 9.65 –

–

Isoleucine Ile I 131.18 C6H13NO2 C6H11NO 113.16 2.36 9.60 –

6.02

Leucine Leu L 131.18 C6H13NO2 C6H11NO 113.16 2.36 9.60 – 5.98

Lysine Lys

K 146.19 C6H14N2O2 C6H12N2O 128.18 2.18 8.95 10.53 9.74

Methionine Met M 149.21 C5H11NO2S C5H9NOS 131.20 2.28 9.21 –

5.74

Phenylalanine Phe F 165.19 C9H11NO2 C9H9NO 147.18 1.83 9.13 –

5.48

Proline Pro P 115.13 C5H9NO2 C5H7NO 97.12 1.99 10.60 – 6.30

Pyroglutamatic Glp U 139.11 C5H7NO3 C5H5NO2 121.09 – – –

5.68

Serine Ser S 105.09 C3H7NO3 C3H5NO2 87.08 2.21 9.15 – 5.68

Threonine Thr T 119.12 C4H9NO3 C4H7NO2 101.11 2.09 9.10 –

5.60
Tryptophan Trp W 204.23 C11H12N2O2 C11H10N2O 186.22 2.83 9.39

– 5.89

Tyrosine Tyr Y 181.19 C9H11NO3 C9H9NO2 163.18 2.20 9.11 10.07

5.66

Valine Val V 117.15 C5H11NO2 C5H9NO 99.13 2.32 9.62 – 5.96

Amino acids are crystalline solids which have the capacity to dissolve in water. Meanwhile, they only
dissolve sparingly in organic solvents, and the extent of their solubility depends on the size and nature of
the side chain. Amino acids feature very high melting points - up to 200-300°C with other properties
varying for each particular amino acid.

20 Amino Acids and their Functions

Only twenty amino acids are most normally found as compounds of human peptides and proteins. These
naturally occurring amino acids are used by cells so as to synthesize peptides and proteins. They are
typically identified by this rather generic formula: H2NCHRCOOH.

The primary difference among the twenty amino acids is the structure of the R group. So, next we will
take a close look at the 20 essential amino acids and their respective functions.

Non-polar, aliphatic residues

Glycine (G/Gly). Slices DNA in order to produce different amino acids. One of the three most important
glycogenic amino acids. Read more about Glycine.

Alanine (A/Ala). Important source of energy for muscle. One of the three most important glycogenic
amino acids. The primary amino acid in sugar metabolism. Boosts immune system by producing
antibodies. Read more about Alanine.

Valine (V/Val). Essential for muscle development. Read more about Valine.

Leucine (L/Leu). Beneficial for skin, bone and tissue wound healing. Read more about Leucine.
Isoleucine (I/Ile). Necessary for the synthesis of hemoglobin. Read more about Isoleucine.

Proline (P/Pro). Critical component of cartilage; aids in joint health, tendons and ligaments. Keeps heart
muscle strong. Read more about Proline.

Aromatic residues

Phenylalanine (F/Phe). Beneficial for healthy nervous system. It boosts memory and learning. Read more
about Phenylalanine.

Tyrosine (Y/Tyr). Precursor of dopamine, norepinephrine and adrenaline. Increases energy, improves
mental clarity and concentration, can treat some depressions. Read more about Tyrosine.

Tryptophan (W/Trp). Necessary for neurotransmitter serotonin (synthesis). Effective sleep aid, due to
conversion to serotonin. Reduces anxiety and some forms of depression. Treats migraine headaches.
Stimulates growth hormone. Read more about Tryptophan.

Polar, non-charged residues

Serine (S/Ser). One of the three most important glycogenic amino acids, the others being alanine and
glycine. Maintains blood sugar levels, and boosts immune system. Myelin sheaths contain serine. Read
more about Serine.

Threonine (T/Thr). Required for formation of collagen. Helps prevent fatty deposits in liver. Aids in
antibodies' production. Read more about Threonine.

Cysteine (C/Cys). Protective against radiation, pollution, and ultra-violet light. Detoxifier; necessary for
growth and repair of skin. Read more about Cysteine.

Methionine (M/Met). An antioxidant. Helps in breakdown of fats and aids in reducing muscle
degeneration. Read more about Methionine.
Asparagine (N/Asn). One of the two main excitatory neurotransmitters. Read more about Asparagine.

Glutamine (Q/Gln). Essential for helping to maintain normal and steady blood sugar levels. Helps muscle
strength and endurance. Gastrointestinal function; provides energy to small intestines. Read more about
Glutamine.

Positively charged residues

Lysine (K/Lys). Component of muscle protein, and is needed in the synthesis of enzymes and hormones.
It is also a precursor for L-carathine, which is essential for healthy nervous system function. Read more
about Lysine.

Arginine (R/Arg). One of the two main excitatory neurotransmitters. May increase endurance and
decrease fatigue. Detoxifies harmful chemicals. Involved in DNA synthesis. Read more about Arginine.

Histidine (H/His). Found in high concentrations in hemoglobin. Treats anemia; has been used to treat
rheumatoid arthritis. Read more about Histidine.

Negatively charged residues

Aspartate (D/Asp). Increases stamina and helps protect the liver; DNA and RNA metabolism; immune
system function. Read more about Aspartate.

Glutamate (E/Glu). Neurotransmitter that is involved in DNA synthesis. Read more about Glutamate.