NAME: _________________________________ RATING: ________________________

GROUP NO. ____________________________ DATE: ________________________

ACTIVITY 10

AMINO ACIDS

Amino acids are organic molecules that, when linked together with other amino
acids, form a protein. Amino acids are essential to life because the proteins they form are
involved in virtually all cell functions. Some proteins function as enzymes, some
as antibodies, while others provide structural support. Although there are hundreds of amino
acids found in nature, proteins are constructed from a set of 20 amino acids.

Each of the 20 most common amino acids has its specific chemical characteristics
and its unique role in a protein structure and function. For example, based on the propensity
of the side chain to be in contact with water, amino acids are classified as hydrophobic (low
propensity to be in contact with water), polar and charged (energetically favorable contact
with water). The charged amino acids include two basic, lysine and arginine (+ charge), and
two acidic, aspartate and glutamate (- charge). Polar amino acids include serine and
threonine (contain a hydroxyl group), asparagine and glutamine (contain amide group).
Histidine is also a polar residue, although its behavior depends on the polarity of its
environment. It has two –NH group with a pKa value of around 6. When both groups are
protonated, the side chain has a charge of +1. However, the pKa may be modulated by the
environment inside the protein, and when raised the side chain may give away a proton,
loosing its positive charge and becoming neutral. By other words, histidine may easily give
away and accept a proton, making it especially useful within enzyme active sites. The
aromatic residues tyrosine and tryptophan and the non-aromatic methionine are often called
amphipathic due to their ability to have both polar and non-polar character. These residues
are often found close to the surface of proteins. The –OH group of tyrosine is able to both
donate and accept a hydrogen bond. The side chains of histidine, tyrosine, phenylalanine
and tryptophan are also able to form weak hydrogen bonds of the types, OH-π and CH-O,
by other words using electron clouds within their ring structures.

The hydrophobic amino acids include alanine, valine, leucine, isoleucine, proline,
phenylalanine, cysteine and methionine. These residues participate in van der Waals type
of interactions. The classification above is based on the type of the amino acid side chain.
However, glycine, being one of the common amino acids, does not have a side chain and
for this reason it is not straightforward to assign it to one of the above classes. Generally,
glycine is often found at the surface of proteins, within loop- or coil (without defined
secondary structure) regions, providing high flexibility to the polypeptide chain at these
locations. This suggests that it is rather hydrophilic. Proline, on the other hand, is generally
non-polar and is mostly found buried inside the protein, although similarly to glycine, it is
often found in loop regions. In contrast to glycine, proline provides rigidity to the polypeptide
chain by imposing certain torsion angles on the segment of the structure. The reason for
this is discussed in the section on torsion angles. Glycine and proline are often highly
conserved within a protein family since they are essential for the conservation of a particular
protein fold.
I. LEARNING OBJECTIVES:

At the end of the exercise, the students should be able to

1. Differentiate essential and Non-essential amino acids

2. Enumerate functions of Amino Acids

3. Categorize the different types of amino acids according to their chemical structures.

4. Identify the function/s and sourced of the different types of amino acids.

5. Understand terminologies related to amino acids.

II. MATERIALS

Work sheet Biochemistry book E-article/E-book on Biochemistry

III. PROCEDURES

1. Answer the following research questions.

2. Fill up the table provided.
3. Define the following terminologies.

IV. RESEARCH QUESTIONS

1. Differentiate essential amino acids to non-essential amino acids.

 An essential amino acid, or indispensable amino acid, is an amino acid that
cannot be synthesized by the organism at a rate commensurate with its demand,
and thus must be supplied in its diet. Non-essential amino acid is any of various
amino acids that are required for normal health and growth, that can be
synthesized within the body or derived in the body. Nonessential amino
acids can be made by the body, while essential amino acids cannot be made by
the body so you must get them from your diet.

2. Enumerate functions of Amino acids

 Amino acids, often referred to as the building blocks of proteins, are compounds
that play many critical roles in your body.
 They're needed for vital processes like the building of proteins and synthesis of
hormones and neurotransmitters.
 Some may also be taken in supplement form for a natural way to boost athletic
performance or improve mood.
 They’re categorized as essential, conditionally essential or nonessential
depending on several factors.
 3. Fill up the table.
Essential/Non- Chemical Characteristics Function/s Sources
Amino Acids Essential
Histidine Essential Histidine has a Histidine is used to Meat
- His - H chemical structure of produce histamine, a Fish
C6H9N3O2. This neurotransmitter that is Poultry
amino acid has a vital to immune Nuts
ring structure that response, digestion, Seeds
Whole grains
contains two nitrogen sexual function and
and is positively sleep-wake cycles. It’s
charged. critical for maintaining
the myelin sheath, a
protective barrier that
surrounds your nerve
cells.
Isoleucine Essential It is an aspartate family The last of the three Eggs
- Ile - I amino acid, a branched-chain amino Soy
proteinogenic amino acids, isoleucine is Protein
acid, an isoleucine and involved in muscle Seaweed
a L-alpha-amino acid. metabolism and is Turkey
Chicken
It is a tautomer of heavily concentrated in
Lamb
aL muscle tissue. It’s also Cheese
isoleucine zwitterion. important for immune Fish
from ChEBI. An function, hemoglobin
essential branched- production and energy
chain aliphatic amino regulation
acid found in many
proteins.
Leucine Essential Leucine is a branched- Leucine is a branched- Meat
Leu– L chain amino acid that chain amino acid that is Fish
consists of glycine in critical for protein Poultry
which one of the synthesis and muscle Eggs
hydrogens attached to repair. It also helps Cheese
Lentils
the alpha-carbon is regulate blood sugar
Nuts
substituted by an levels, stimulates Seeds
isobutyl group. wound healing and
produces growth
hormones
Lysine Essential It is the side chain that Lysine plays major Red meat
- Lys – K is specific to each roles in protein Parmesan
amino acid. The synthesis, hormone and Sardines
specific structure of lysi enzyme production and
ne is indicative of its the absorption of  Eggs.
chemical formula, calcium. It’s also  Soybeans
C6H14N2O2.Lysine is important for energy  Tofu
a linear amino acid production, immune  Spirulina
 molecule. Lysine is a function and the  Fenugreek
base, much like production of collagen seed
arginine and histidine. and elastin.

Methionin Essential It is one of two amino Methionine plays an Eggs

e acids that contain the important role in Meat
Met – M element sulfur; the metabolism and Sesame
other is cysteine. The detoxification. It’s also Seeds
chemical formula necessary for tissue Brazil nuts
of methionine is growth and the Some plant
C5H11NO2S. In absorption of zinc and seeds
general, all amino selenium, minerals that Cereal
acids have the are vital to your health. grains
same structure: an
amino group attached
to a hydrogen, a
carboxyl group and a
side chain group,
denoted by 'R' via a
central carbon.
Phenylalani Essential It is an erythrose 4- Phenylalanine is an Beef
ne phosphate/phosphoen amino acid found in Poultry
- Phe - F olpyruvate family many foods and used Fish
amino acid, a by your body to Milk
proteinogenic amino produce proteins and Yogurt
acid, other important Eggs
a phenylalanine and a molecules. It has been Cheese
L-alpha-amino acid. It studied for its effects on Soy
is a conjugate base of depression, pain and products
a L-phenylalaninium. ... skin disorders.
It is an enantiomer of a
D-phenylalanine. It is a
tautomer of a L-
phenylalanine zwitterio
n.
Threonine Essential Threonine is one of Threonine is a principal Cottage
Thr - T two proteinogenic part of structural Cheese
amino acids with two proteins such as Poultry
chiral centers, the collagen and elastin, Fish, Meat
other being which are important Lentils
isoleucine. Threonine c components of the skin Black turtle
an exist in four and connective tissue. bean
possible stereoisomers It also plays a role in fat Sesame
with the following metabolism and seeds
configurations: immune function
(2S,3R), (2R,3S),
 (2S,3S) and (2R,3R).
Tryptopha Essential The official makeup Though often  Salmon.
n of tryptophan is associated with causing This oily
- Trp - W drowsiness, tryptophan fish is also
(2S)-2-amino-3-
has many other  Poultry
(1H-indol-3-yl) functions. It’s needed to
propanoic acid. Eggs
maintain proper
nitrogen balance and is Spinach
a precursor to  Seeds
serotonin, a  Milk
neurotransmitter that  Soy
regulates your appetite, products
sleep and mood
 Nuts.

Essential/No Chemical Function/s Sources

Amino Acids n-Essential Characteristics
Valine Essential Valine is a branched- Valine is one of three Meats
- Val - V chain amino acid that branched-chain amino Dairy
consists of glycine in acids, meaning it has products
which one of the a chain branching off Soy products
Beans
hydrogens attached to to one side of its
Legumes
the alpha-carbon is molecular structure.
substituted by an Valine helps stimulate
isopropyl group. It has muscle growth and
a role as a plant regeneration and is
metabolite and a involved in energy
Daphnia magna production
metabolite. It is a
branched-chain amino
acid and an alpha-
amino acid.
Alanine Non- Alanine is an aliphatic Removes toxic Meat
- Ala - A essential amino acid, because substances released Poultry
the side-chain from breakdown of Fish
connected to the α- muscle protein during
carbon atom is a intensive exercise.
methyl group (- Side effects:
CH3); alanine is the Excessive alanine
simplest α-amino acid level in the body is
after glycine. associated with
chronic fatigue.
Arginine Non- Arginine, also known Arginine plays an  Nuts
- Arg - R essential as l-arginine (symbol important role in cell  Seeds
 Arg or R), is an α- division, wound  Meat
amino acid that is used healing, removing products
in the biosynthesis of ammonia from the  Legumes
proteins. It contains an body, Chickpeas
α-amino group, an α- immune function, and Seaweeds
carboxylic acid group, the release of
and a side chain hormones. It is a
consisting of a 3- precursor for the
carbon aliphatic synthesis of nitric
straight chain ending in oxide (NO), making it
a guanidino group. important in the
regulation of blood
pressure.
Asparagine Non- It is an aspartate family Asparagine is known  Dairy
- Asn - N essential amino acid, a for its key role in the  Eggs
proteinogenic amino biosynthesis of  Whey
acid, glycoproteins. In
an asparagine and a L- addition, it is also  Beef
alpha-amino acid. ... It essential for the  Poultry
is a conjugate acid of a synthesis of many  Seafood
L-asparaginate. It is an other proteins. Human  Potatoes
enantiomer of a D- nervous system also
 Nuts
asparagine. It is a needs this amino acid
tautomer of a L- to be able to maintain Seeds
asparagine zwitterion. an equilibrium  Soy
products
Non- It is an aspartate Enhances stamina, Oysters
Aspartic acid essential family amino acid, a aids in removal of Sausage
- Asp - D proteinogenic amino toxins and ammonia Meat
acid, an aspartic from the body, and Sprouting
acid and a L-alpha- beneficial in the seeds
amino acid. It is a synthesis of proteins Oat flakes
Avocado
conjugate acid of a L- involved in the
Asparagus
aspartate(1-). It is an immune system. Young
enantiomer of a D- sugarcane
aspartic acid. One of
the non-
essential amino
acids commonly
occurring in the L-form.
Cysteine Non- Cysteine (symbol Cys Component Chicken
- Cys - C essential or C is a semi- of protein type Turkey
essential proteinogenic abundant in nails, skin Yogurt
amino acid with the and hair. It acts Cheese
formula as antioxidant (free Eggs
sunflower
HO2CCH(NH2)CH2SH. radical scavenger),
seeds
 The thiol side chain and has synergetic Legumes
in cysteine often effect when taken with
participates in other antioxidants
enzymatic reactions, such as vitamin
as a nucleophile. E and selenium.
Non- Glutamic acid is a non- Glutamic acid has Poultry
Glutamic acid essential essential amino several Fish
- Glu - E acid that forms key functions within Eggs
proteins. This amino the body. It acts as an Dairy
acid has a chemical important products
Kombu
formula of C5H9NO4. neurotransmitter and
Glutamic acid has the the body uses it to
normal amino acid create other
structure of an amino neurotransmitters,
acid: amine group, such as GABA. Thus,
central carbon, this amino acid is
carboxylic group and critical for healthy
an R group. brain development
and function.

Amino acids Essential/no Chemical characteristics Function/s Sources

n
essential
Glutamine Non- The amino and Glutamine is  Meat
- Gln - Q essential carboxyl groups and produced in the  Seafood
central carbon are muscles and is  Milk
considered the amino distributed by the
acid backbone and are blood to the organs  Nuts
the same in all amino that need  Eggs
acids. It is the side it. Glutamine might  Cabbage
chain that is specific to help gut function, the  Protein
each amino acid. The immune system, and Drinks
specific structure of glu other essential
 Beans
tamine is indicative of processes in the
its chemical formula, body, especially in
C5H10N2O3. times of stress.
... Glutamine is a linear
molecule and polar in
nature.
Glycine Non- Glycine symbol Gly or Is used to help create Meat
- Gly– G essential G is an amino acid that muscle tissues and  Fish
has a single hydrogen convert glucose into  Dairy
atom as its side chain. energy. In addition, it products
It is the simplest amino is also vital for
 acid (since carbamic maintaining healthy  Legumes
acid is unstable), with central nervous and
the chemical formula digestive systems.
NH2‐CH2‐COOH. Glyci
ne is one of the
proteinogenic amino
acids. ... Glycine is a
colorless, sweet-
tasting crystalline solid.
Proline Non- The distinctive Plays role in  Pork
- Pro - P essential cyclic structure of proli intracellular Products
ne's side chain signalling. It is vital  Lamb
gives proline an for  Veal
exceptional proper functioning of
conformational rigidity Sausages
joints and tendons. Luncheon
compared to other Besides, this amino
amino acids. It also Meats
acid helps maintain
affects the rate of  Dairy and
and strengthen heart
peptide bond formation Egg Products
muscles.
between proline and  Soups
other amino acids. Sauces
 Gravies
 Snacks
Serine Non- It is a serine family Constituent of brain Soybeans
- Ser - S essential amino acid, a proteins and aids in Nuts
proteinogenic amino the synthesis of Peanuts
acid, a L-alpha-amino immune system Almonds
acid and a serine. It is proteins. It is also Walnuts
Eggs
a conjugate base of a good for muscle
Chickpeas
L-serinium. A non- growth. Serine is Lentils
essential amino acid needed for the Meat
occurring in natural metabolism of fats, Shellfish
form as the L-isomer. It fatty acids, and cell
is synthesized from membranes
glycine or threonine.
Tyrosine Non- L-Tyrosine is the Is thought to increase Chicken
- Tyr - Y essential levorotatory isomer of levels of the neuro Fish
the aromatic amino transmitters dopamine, Yogurt
acid tyrosine. ... It is an adrenaline and Cheese
erythrose 4- norepinephrine. By Peanuts
phosphate/phosphoenol increasing these Pumpkin
pyruvate family amino neurotransmitters, it Sesame seeds
acid, a proteinogenic may help improve Soy products
amino acid, memory and Milk
Turkey
a tyrosine and a L- performance in
alpha-amino acid. stressful situations
4. Define the following terms
a. Glucogenic amino acids.
 A glucogenic amino acid is an amino acid that can be converted into
glucose through gluconeogenesis. This is in contrast to the
ketogenic amino acids, which are converted into ketone bodies.

b. Ketogenic amino acids.

 Ketogenic amino acids are unable to be converted to glucose as both
carbon atoms in the ketone body are ultimately degraded to carbon
dioxide in the citric acid cycle.

c. Acidic amino acids.

 An amino acid is a type of organic acid that contains a carboxyl functional
group (-COOH) and an amine functional group (-NH2) as well as a side
chain (designated as R) that is specific to the individual amino acid.

d. Basic amino acids

 An amino acid is an organic molecule that is made up of a basic
amino group (−NH2), an acidic carboxyl group (−COOH), and an organic R
group (or side chain) that is unique to each amino acid. The term amino
acid is short for α-amino [alpha-amino] carboxylic acid.

e. Peptides
 a compound consisting of two or more amino acids linked in a chain, the
carboxyl group of each acid being joined to the amino group of the next by
a bond of the type -OC-NH-.

f. Methionine.
 Methionine is an amino acid. Amino acids are the building blocks that our
bodies use to make proteins. Methionine is found in meat, fish, and dairy
products. It plays an important role in the many functions within the body.

g. Tryptophan
 Tryptophan is an amino acid needed for normal growth in infants and for
nitrogen balance in adults. It is an essential amino acid. This means your
body cannot produce it, so you must get it from your diet.
 h. Aminotransferase.
 Aminotransferases or transaminases are a group of enzymes that catalyze
the interconversion of amino acids and oxoacids by transfer of amino
groups.

V. REFERENCE/S:

 https://www.medicinenet.com/script/main/art.asp?articlekey=22839
 https://www.merriam-
webster.com/dictionary/nonessential%20amino%20acid
 https://www.healthline.com/nutrition/essential-amino
acids#targetText=Amino%20acids%2C%20often%20referred%20to,synth
esis%20of%20hormones%20and%20neurotransmitters.
 https://www.ncbi.nlm.nih.gov/pubmed/31096630
 https://www.dietaryfiberfood.com/amino-acids/non-essential-amino-
acids.php
 https://www.asi.k-state.edu/research-and-
extension/swine/swinenutritionguide/essentialandnonessentialaminoacids.
html
 https://www.medicalnewstoday.com/articles/324229.php
 https://www.healthline.com/nutrition/phenylalanine#targetText=Phenylalani
ne%20is%20an%20amino%20acid,depression%2C%20pain%20and%20s
kin%20disorders.
 https://www.myfooddata.com/articles/high-tyrosine-foods.php
 https://pubchem.ncbi.nlm.nih.gov/compound/Tyrosine#targetText=L%2DT
yrosine%20is%20the%20levorotatory,the%20aromatic%20amino%20acid
%20tyrosine.&targetText=It%20is%20an%20erythrose%204,L%2Dalpha%
2Damino%20acid.
 https://aminoacidsguide.com/Pro.html#targetText=What%20is%20the%20
role%20of,maintain%20and%20strengthen%20heart%20muscles.
 https://pubchem.ncbi.nlm.nih.gov/compound/Serine#targetText=It%20is%
20a%20serine%20family,base%20of%20a%20L%2Dserinium.&targetText
=A%20non%2Dessential%20amino%20acid%20occurring%20in%20natur
al%20form%20as,synthesized%20from%20glycine%20or%20threonine.