Amino Acids

Amino acids are the building blocks of proteins. The precise amino acid content, and the
sequence of those amino acid, of a specific protein is determined by the sequence of the bases in
the gene that encodes that protein.
Structure, Components and Properties of Amino Acids
Amino acid contains at least one of the both amino and carboxylic acid functional groups.
R

H 2N C COOH

H
The N- terminal end of amino group (-NH2) and the C-terminal end carboxyl group (-COOH)
bond to -carbon, with the amino group of one amino acid linking with the carboxyl group of
another, forming a peptide bond. The chains of amino acids is known as polypeptide, and a large
polypeptide constituent a protein.
Amino acid differ from each other by the chemical composition of their R group (side
chains). The R group found on the 20 different amino acids used in building proteins.

AMINO ACIDS

Glysine Glutamine

Alanine Serine

Valine Threonine

Leucine Tyrosine

Isoleucine Lysine

Cysteine Arginine

Methionine Histidine

Tryptophan Aspartate

Phenylalanine Glutamate

Asparagine Proline

Protein
Proteins, from the Greek proteios, meaning first, are a class of organic compounds which
are present in and vital to every living cell. In the form of skin, hair, callus, cartilage, muscles,
tendons and ligaments, proteins hold together, protect, and provide structure to the body of a
multi-celled organism. In the form of enzymes, hormones, antibodies, and globulins, they
catalyze, regulate, and protect the body chemistry. In the form of hemoglobin, myoglobin and
various lipoproteins, they effect the transport of oxygen and other substances within an
organism.
Structure, Components and Properties of Proteins
Proteins are polymers specifically polypeptides sequence formed from L--amino acids.
Each unit of a protein is called amino acid residue. There are four distinct levels of a proteins
structure which are the primary, secondary, tertiary and quaternary.
Proteins also consist of the elements carbon, nitrogen, oxygen, hydrogen and sulfur. The
nitrogen content of serum protein in average is approximately 16%. This measurement of
nitrogen content is used in one method for total protein. Proteins can be positively and
negatively charged because they contain many ionizable group on the side chains of their amino
acids and their N- and C-terminal ends.
Isoelectric point (pl) is when there is no net charge in amino acids or protein pH levels.
When the pH > pl, a protein has a net negative charge, and when the pH < pl, a protein has a
positive charge.

PROTEIN STRUCTURE
Four Levels of Protein Structure
1. Primary structure represents the number and type of amino acids in the specific amino
acid sequence.
2. Secondary structure regularly repeating structures stabilized by hydrogen bonds
between the amino acids within the protein. Common secondary structures are the -helix,
-pleated sheet, and most serum forming a helix.
3. Tertiary structure refers to overall shape, or conformation, of the protein molecule. This
conformation is known as the fold, or the spatial relationship of the secondary structure to
one another. Tertiary structures are three-dimensional. Tertiary structures results from the
interaction of side chains and is stabilized through the hydrophobic effect, ionic attraction,
hydrogen bonds, and disulfide bonds.
4. Quaternary structure the shape or structure that results from the interaction of more
than one protein molecule, or protein subunits, held together by noncovalent forces such
as hydrogen bonds and electrostatic interactions, which are part of the larger protein
complex with a precise three-dimensional configuration.

PROTEIN METABOLISM
Most plasma proteins are synthesized in the liver and secreted by the hepatocytes into the
circulation. It is the information encoded in the gene, specified by the nucleotide sequence that
provides each protein with its own amino acid sequence. Protein metabolism starts at the
unfolding of double-stranded DNA in the nucleus and one strand is used as template for the
formation of a complementary strand of mRNA. This process is called transcription. The mRNA is
then used as template for protein synthesis by the ribosomes. It is manufactures in the cell
membrane and then translocated across the nuclear membrane into the cytoplasm where it
attached to the ribosomes for the protein synthesis to take place.
Translation is the process of synthesizing a protein from an mRNA template. The mRNA is
loaded onto the ribosome and is read by three nucleotide at a time by matching each codon to
its base pairing anticodon located on a tRNA molecule, which carries the amino acid
corresponding to the codon it recognizes to the ribosome. This process continues until the mRNA
message is read and all amino acid are in the specific sequence to form the polypeptide chain.
The code on the mRNA also contains initiation and termination codons for the peptide chain.
The next step in protein synthesis is getting the amino acids to the ribosomes. First, the
amino acid is activated in the reaction that requires energy and specific enzyme for each amino
acid. This activated amino acid complex is then attached to another kind of RNA, tRNA, with the
subsequent release of activating enzyme and adenosine monophosphate. The tRNA is a short
chain of RNA that occurs free in the cytoplasm. Each amino acid has a specific tRNA that contain
three bases that corresponds to the three bases in the mRNA. The tRNA carries is particular
amino acid to the ribosome and attached to the mRNA in accordance with the matching codon.
In this manner, the amino acids are aligned in sequence. As each new tRNA brings in the next
amino acid, the preceding amino acid is transferred onto the amino group of new amino acid and
enzymes located in the ribosomes form a peptide bond. The tRNA is released in the cytoplasm,
where it can pick up another amino acid, and the cycle repeats. When the terminal codon is
reached, the peptide chain is detached and the ribosome and mRNA dissociate.
ESSENTIAL AND NON-ESSENTIAL AMINO ACIDS
Essential Amino Acids
Arginine complex amino acid that is often found at the catalytic (active) site in proteins
and enzyme due to its amine-containing side chain. It plays an important role in cell
division, healing of wounds, stimulation of protein synthesis, immune function, and release
of hormones and generation of urea or urine.
 Histidine one of the basic (by pH) amino acids due to its imidazole side chain. It is the
direct precursor of histamine, one of the protein involved in immune response. Histidine is
also important source of carbon atoms in the synthesis of purine, one of the two groups of
nitogen bases that make up DNA and RNA. It is also needed in growth and repair of
damage tissues and to maintain myelin sheaths that protects the nerve cells.
Isoleucine group of branched-chain amino acids that are needed to maintain, heal, and
repair muscle tissues, skin and bones. It is needed for the hemoglobin formation and
regulation of blood glucose levels.
Leucine group of branched-chain amino acids and the second most common amino acid
found in the protein. It boost healing of muscles, skin and bones; aids recovery from
surgery; and lowers blood glucose levels.
Lysine has net positive charge, which makes it one of the three basic (by charge) amino
acids. It plays a role in production of antibodies, lowers triglyceride levels and helps in
absorption and conservation of calcium.
Methionine an important amino acid that helps to initiate translation of messenger RNA
by being the first amino acid to incorporated into the N-terminal position of all protein. It is
the source of sulfur, assists the breakdown of fats, help to detoxify lead and other heavy
metals, help diminish muscle weakness and prevent brittle hair.
Phenylalanine a nonpolar amino acid because of the hydrophobic nature of benzyl side
chain. It promotes alertness and vitality, elevates mood, decreased pain, aids in memory
and learning, and used to treat arthritis and depression.
Threonine a alcohol-containing amino acid that is an important component in the
formation of protein, collagen, elastin and tooth enamel. It is important in the production
of neurotransmitters and health of the nervous system.
Tryptophan formed from proteins during digestion by the action of proteolytic enzymes. It
is the precursor for serotonin and melatonin, a neurohormone and powerful antioxidant. It
is also a natural relaxtant; it helps alleviate insomnia, soothes anxiety, and reduces
depression.
Valine a branched-chain amino acid that is constituent of fibrous protein in the body. It is
needed in the muscle metabolism and coordination, tissue repair and maintenance of
nitrogen balance.

Non-essential Amino Acids

Alanine one of the simplest amino acids and is involved in the energy-producing
breakdown of glucose. It plays important role in transfer of nitrogen from peripheral
tissues to the liver, helps in reducing the buildup of toxic substance and strengthens
immune system.
Asparagine first isolated in the asparagus juice, becoming the first amino acid to be
isolated. It is one of the principal and frequently the most abundant of the amino acids
involved in the transport of nitrogen. Its main function are converting one amino acid into
another via amination, synthesis of ammonia and transamination.
Aspartic Acid is an alanine with one of the -hydrogens replaced by a carboxylic acid
group. It plays the vital role in metabolism during the construction of other amino acids
and metabolites in the citric acid cycle.
Cysteine an important structural and functional component of many protein and
enzymes. Although it is nonessential amino acid, but it may be essential for infants, the
elderly, and the individuals with certain metabolic disorders and malabsorption
syndromes.
Glutamic Acid synthesized from a number of amino acids, and when an amino group is
added to glutamic acid, it forms the important amino acid glutamine. It serves as
neurotransmitter and its dysregulation has been linked to epileptic seizures. It is also often
used as a food additive and flavor enhancer in the form of its sodium salt, monosodium
glutamate.
Glutamine most abundant amino acid in the body. It is being involved in more metabolic
process than any other amino acids. It assists in maintaining the proper acid/alkaline
 balance in the body, provides fuel for a healthy digestive tract, and is the basis of the
building blocks for the synthesis of RNA and DNA.
Glycine simplest amino acid synthesized in the body and is the only amino acid that is
not optically active because it has no stereoisomers. It is essential for the synthesis of
nucleic acid, bile acids, proteins, peptides, purines, ATP, porphyrins, hemoglobin,
glutathione, creatine, blie salts, glucose, glycogen and other amino acids. It has also sweet
taste and is used as a sweetener/taste enhancer.
Proline precursor of hydroxyproline, which is manufactured into ligaments, collagen,
tendons, and heart muscle of the body. It involves in the wound healing, plays important
role in molecular recognition, and healing of cartilage and strengthening of joints and
tendons.
Serine second amino acid that is also an alcohol because of its methyl side chain, which
contains a hydroxyl group. It is needed for proper metabolism of fats and fatty acids and
plays an important role in the bodys synthetic pathways for pyrimidines, purines,
creatine, and porphyrins.
Tyrosine metabolically synthesized from the important amino acid phenylalanine to
become the para-hydroxy derivative of phenylalanine. It aids in the function of adrenal,
thyroid, pituitary glands, and acts as mood elevator, suppressed appetite, and help in
reducing body fats. It is also a precursor of adrenal hormones epinephrine, norepinephrine,
and dopamine and the thyroid hormones, including thyroxine.