REFERENCES HOW DO THEY CREATE ATP?

• PPT1A (CANVAS) • The big molecule here orchestrates the ATP

• PPT1B (CANVAS) synthesis
• Video Discussions
• Lehninger Book The ions in the picture:
• Other Online Videos

TOPIC

BIOCHEMISTRY

- is the chemistry of life. It aims to explain biological

form and function in chemical terms. Biochemistry
describes in molecular terms the structures, (Ions are the one in the red circle, you may refer to
mechanisms, and chemical processes shared by the video link to further view the whole ATP)
organisms.
THE IONS CREATE ENERGY
WHAT DISTINGUISHES LIVING ORGANISMS FROM
INANIMATE OBJECTS?

The degree of chemical complexity and organization >>

chemistry, cell biology
Organisms extract, transform and use energy from their
environment >> bioenergetics, physics
The ability to self-replicate and self-assemble >> genetics,
evolution
Biochemistry is just the bigger picture of organic chemistry. • Once linked together, it creates cascades of event
in a molecular level (pic above)
• This molecule generates ions in the process.
CHEMISTRY OF LIFE
THE ROTARY MOTION
GENERATES IONS:
ATPase in Action

• The picture below shows ATP synthase:

It means it will
synthesize the
ATP.

• Because of these biomolecules can actually

perform different biochemical reaction inside
our system.
 • Carbon can perform with a single bond; it can be
rotated. You can rotate if it is a single bond, if it
LEARNING A LANGUAGE is a double bond (letter b on the image), it is not
possible to be rotated (letter c on the image).
• Learning biochemistry is like learning a • If you have 2-3 bonds it is not possible to rotate,
language it is fixed to its position.
• The book: Lehninger Principles of
Biochemistry (by: David L. Nelson & Michael
M. Cox)
A STEREOCHEMISTRY CAN BE A:
THE ALPHABET OF LIFE CIS CONFIGURATION TRANS CONFIGURATION
is on the same side (if the is on the opposite (if one
• Since biochemistry is like learning a new functional group or R of the functional group or
language, we have the alphabet of having the group is in the upper side, R group is in the upper
table of elements. as well as the other one side, the other functional
group or R group is in the
lower side)

AMINO ACIDS
- Known as the building blocks of proteins

CARBON

• The main letter that is used in biochemistry is

the letter “C” (carbon).
• Carbon’s configuration is tetrahedron
• How many bonds can carbon contain? 4
bonds

HONC RULE

Hydrogen 1 bond
Oxygen 2 bonds
Nitrogen 3 bonds Once all this words once they ate joined together, they
Carbon 4 bonds can become a polymer and this polymer can become a
sentence.
 Once they arrive in repeating units • If there is a bond in the
they can act as a polymer (like a amino acids they can act as
plastic) stereoisomers, the
stereoisomers of the
If the monomer or the building amino acids are called
Monomer blocks ex. Amino acids joined enantiomers.
together it can be a protein, a sugar • They have the ability to
can become a cellulose or a reflect and bend light. -
polysaccharide, and a nucleotide Amino acids that contains
can become a DNA disulfide bonds is
(Deoxyribonucleic Acid). CYSTEINS.
Once they are combined the DNA
can become a chromatin, the
protein can become a plasma
membrane, and the cellulose can
become a cell wall.

Combining all of the Supra

Molecular complexes it creates the
cell and its organelles.

The cell won’t become a cell • The law that absorbs UV:
without starting with the building Lambert-Beer law
blocks (monomeric units).

Macromolecul
es

Refer to this picture upon reading the explanation

Amino acids are Enantiomers, they have 2

stereoisomers left or right.
L-Amino Acids
The e. Coli is made up of 70% of L means levorotatory; (L- if amino group is on the left
water, same with us people made side)
up of 70% of water. D means Dextrorotatory; (D-if amino group is on the
E. coli
right side)
 • The side chains (R) are your functional group,
dependent on the functional group decides
which ever amino acids class it belongs.

• C means carbon, it has an alpha (the chiral

carbon) if there are 4 different species that is
bonded to the carbon.

CHIRAL MOLECULE ABSOLUTE CONFIGURATION

• Rotated molecule cannot be superimposed
on its mirror image. - arrangement of atoms in chiral molecules that
• Optically active distinguishes the right-handed and left-handed stereo
structures

ACHIRAL MOLECULE - rotated molecule can be

superimposed on its mirror image.

OPTICAL ACTIVITY
D AND L ENANTIOMERS
- configurational stereochemistry of the molecule.

- 3Rotation to the left (from the viewer’s POV) is

designated by the prefix (-), rotation to the right by the
prefix (+).
 RACEMATES L-ALLOISELUCINE
- mixtures containing equal concentrations of L- and
- it is the L-isomer with the opposite configuration at
D- forms [(-) and (+)].
C3.
- optically inactive
NOTE: Glycine is not chiral. Isoleucine has two chiral
DIASTEREOMERS centers

- molecules with more than one chiral center.

- can be optically active.

20 AMINO ACIDS
- occur proteins.
- all chiral amino acids that occur in proteins have L
configuration.
- can be grouped according to the chemical nature of
their side chains called R groups.

- Histidine is conditionally positively charged.

POLAR, UNCHARGED R GROUPS

Asparagus - named
after Asparagine due to
the high amount of the
non-essential amino
acid.
 AROMATIC R GROUPS ABSORBANCE AND ABSORPTION OF COEFFICIENTS
LAMBERT-BEER LAW
Turkey - is rich in
tryptophan which
improves mood and
sleep.

OXIDATION OF CYSTEINE RESULTS IN DISULFIDE

BOND FORMATION

Example of the relationship of T to A: In 90% of the

incident light is absorbed after 1cm, log (100/1) = 2.0
= A.

LAMBERT BEER-LAW
- A is linearly proportional to c and I.
- 𝜺 is the molar absorption (or extinction) coefficient

ABSORBANCE OF UV LIGHT BY AROMATIC AMINO

ACIDS

(units are M-¹ cm-¹)

APPLICATION: DETERMINATION OF THE

CONCENTRATION.

NONIONIC AND ZWITTERIONIC FORMS

- A zwitterion can act as either an acid or a base.

- Substances that have this property are amphoteric
and are often called ampholytes (amphoteric
electrolytes)
- Free amino acids are zwitterionic at neutral pH.
 AMINO ACID TITRATION, IONIZATION STATES AND 3. pH -
ISOELECTRIC POINT (IEP) negative,
basic

pKa = pK1 = pH of a molecule

- pKa is equal to pH when the solution is neither acidic

nor basic.

This can be seen on the in-betweens of the graph.

- pl ½ (pK₁+pK₂) pl
- pl - The pH at which the net electric charge of a
molecule is at zero. - pH with a net charge of zero
- Can be seen at the midline of the graph (Ex. pI =
5.97)

AMINO ACIDS CAN HAVE 3 FORMULAS (+1, 0, -1)

Example: Glycine

1. pH -
positive,
acidic

2. pH -
neutral
 AMINO ACIDS CAN HAVE 3 FORMULAS (+1, 0, -1) PEPTIDE BOND FORMATION
Example: Glutamate - One amino acid connects to another amino acid
TITRATION CURVE FOR GLUTAMATE through Hydrolysis.
- Peptide = amide

HYDROLYSIS
- The process of breaking chemical bonds with the
GLUTAMATE CAN HAVE 4 FORMS (+1, 0, -1, -2) presence of water.
The net charge value changes when: - Hydration (addition of water)
- its proton is donated - Protein, Product: 2 amino acids Protein to 2 amino
- Concentration changes acids

CONDENSATION
- Dehydration (removal of water)
- 2 amino acids, Product: Protein 2 amino acids to
Protein

AMINO ACID RESIDUE

- The amino acid present in a protein (a product of 2

amino acids)
 OLIGOPEPTIDE FORMATION

EXAMPLE 1

PARTIAL DOUBLE BOND CHARACTER OF PEPTIDE

BONDS
For this example, 6 amino acids were joined through 5
peptide bonds (NH)

When reading a protein, always begin at amino

terminal (N-terminal)

Start (N-Terminal)
- amino terminal (Ex. H2N) The carbonyl oxygen has a partial charge (δ −) and the
amide nitrogen a partial positive charge (δ +), setting
End (C-Terminal) up a small electric dipole.
- carboxyl group (Ex. COOH)
Virtually, all peptide bons in proteins occur in this trans
configuration
EXAMPLE 2

The partial double-bond character makes the peptide

bond planar.
STERIC HINDRANCE IN CIS-PEPTIDE BONDS
1. PRIMARY STRUCTURE
- amino acid residue
- Primary sequence affect primary structure
- Primary structure affect its function

Amino acid
- Primary structure of proteins
2. SECONDARY STRUCTURE

- α helix (alpha) is present

R groups are oriented 3. TERTIARY STRUCTURE

Trans
alternately
- Combination of α helix and β sheath (beta)
R groups are oriented in
Cis - Covalent bond
one direction
Cannot be rotated due to 4. QUARTERNARY STRUCTURE
Steric Hindrance presence of double
bonds - Combination of tertiary structures
- Noncovalent bond (hydrogen bond, nitrogen bond,
disulfide bond, ionic bond, etc.)

METHODS FOR FRAGMENTING POLYPEPTIDE

CHAINS THROUGH CLEAVING

HIERARCHY OF PROTEIN ORGANIZATION

PROTEIN SEQUENCING
 TRYPSIN
- Can digest protein in particular places ex.

- Once those are removed, it will form into peptides.

MASS SPECTROMY

AMINO ACIDS CONTINUATION

- used frequently to achieve high resolution

separation of protein complex mixtures.
- Where:
- E=electron potential
- U=electrophoretic mobility
- V=velocity
- Z=net charge
- f= frictional coefficient
- Therefore: Migration of protein in a gel during
electrophoresis is a function of its size and shape
 TWO-DIMENSIONAL ELECTROPHORESIS
- permits resolution of complex mixture of proteins

- Two-dimensional electrophoresis separates proteins

of identical molecular weight that differ in pI, or
proteins with similar pI values but different molecular
weights

Sodium dodecyl sulfate - a detergent commonly

employed in electrophoresis

- The bound SDS contributes a large net negative

charge

- It partially unfolds proteins - added with dye such as

Coomassie blue which binds to proteins but not the
gel itself

ISOELECTRIC FOCUSING
- Determining the isoelectric point (pI) of protein
- pH gradient is established by allowing a mixture of
molecular weight organic acids & bases to distribute
themselves in an electric field generated across the
gel.
- Each protein migrates until it reaches the pH that
matches its pI.
 ENZYMES PROTEIN STRUCTURE
- All covalent bonds
- The amount in a given solution or tissue extract can (mainly peptide bonds
be measured, or assayed, in terms of the catalytic and disulfide bonds)
effect the enzyme produces—that is, the increase in linking amino acid
the rate at which its substrate is converted to reaction PRIMARY STRUCTURE
residues in a polypeptide
products when the enzyme is present. chain
- Sequence of amino
OPTIMUM TEMPARATURE FOR ENZYMES acids
- 25 - 38 C - Stable arrangements of
- By international agreement, 1.0 unit of enzyme amino acid residues
SECONDARY STRUCTURE which forms recurring
activity for most enzymes is defined as the amount of
enzyme causing transformation of 1.0 umol of structural pattern
substrate to product per minute at 25C under optimal -Three-dimensional
conditions of measurement TERTIARY STRUCTURE
folding of a polypeptide
QUARTERNARY - two or more
STRUCTURE polypeptide subunits
ACTIVITY VS. SPECIFIC ACTIVITY
- activity refers to the total units of enzyme in a
solution
- specific activity is the number of enzyme units per
milligram of total protein (measured by enzyme purity)

IS THE AMINO ACID SEQUENCE ABSOLUTELY FIXED,

OR INVARIANT, FOR A PARTICULAR PROTEIN?
- No; some flexibility is possible. An estimated 20% to
30% of the proteins in humans are polymorphic,
having amino acid sequence variants in the human
population.

- Although the amino acid sequence in some regions

of the primary structure might vary considerably
without affecting biological function, most proteins
contain crucial regions that are essential to their
function and whose sequence is therefore conserved.

MAJOR DISCOVERIES IN 1953

- James D. Watson and Francis Crick deduced the
double-helical structure of DNA and proposed a
structural basis for its precise replication

- Frederick Sanger worked out the sequence of amino

acid residues in the polypeptide chains of the hormone
insulin
 PROTEIN SEQUENCING OVERLOAD

Direct protein - sequencing by Fred Sanger using 1-

fluoro-2,4-dinitrobenzene FDNB, dansyl chloride, or
dabsyl chloride to label aminoterminal group
 PROTEIN SEQUENCING OF EDMAN DEGRADATION PROTEOLYTIC ENZYMES (PROTEASES)
Proteases are enzymes that break down the peptide
bonds of protein (in the body or the skin). These
enzymes are produced by animals, plants and fungi
and bacteria.

Proteases are divided into three; acid, neutral and

alkaline proteases.

Sequences of an amino acid and protein can be

identified through Edman degradation. Developed by
Pehr Edman and was automated in 1967 by Edman
and Beggs

This procedure labels and cleaves the between N-

peptide bonds and other amino acid residues without
disrupting peptide bonds. SO, IF I HAVE TRYPSIN, AND MY POLYPEPTIDE HAS 3
LYSINE RESIDUES, HOW MANY SMALLER PEPTIDES
Edman Degradation procedures labels and removes WILL I YIELD?
only the amino terminal residue of the peptide and ANSWER: 4
leaves the rest of the peptide bond intact.
STEPS Protease is specific while acid-hydrolysis is nonspecific
a. Phenylisothiocyanate reacts with the peptide
The sulfhydryl group on Cys residues can be modified
under mildly alkaline conditions converting the amino-
with iodoacetamides, maleimides, benzyl halides, and
terminal acid phenylthiocarbamoyl PTC adduct.
bromomethyl ketones.
b. The peptide bond next to the PTC adduct is then
cleaved in a step carrying out anhydrous trifluoroacetic
acid. with removal of the amino-terminal amino acid
as an anilinothiazolinone derivative.

c. Organic solvents are used to extract the derivatized

amino acid converted to the more stable
phenylthiohydantoin derivative by treatment with
aqueous acid, and then identified.

[adducts - is formed through direct addition of two

molecules. In biology it is when chemicals bind to
biological molecules.]
 MASS SPECTROMETRY
is an analytical tool used for mass to charge ratio (m/z)
to measure one or more molecules in a sample.

a. For highly accurate measurements of a molecular

weight of a protein
b. Analytes that will be analyzed are ionized first in a
vacuum
c. the newly charged molecules are introduced into an
electric and/or magnetic field, their paths through the
field are a function of their mass to-charge ratio, m/z
MATRIX-ASSISTED LASER DESORPTION/IONIZATION
MASS SPECTROMETRY, OR MALDI MS
is used to analyze extremely large molecules.

- Analyzes synthetic and natural polymers, proteins,

and peptides.
- Directly vaporize and ionize analytes

Proteins are placed in a light-absorbing matrix. With a

short pulse of laser light, the proteins are ionized and
then desorbed from the matrix into the vacuum
system.
ELECTROSPRAY IONIZATION MASS SPECTROMETRY,
OR ESI MS
uses electrical energy for transferring ions of a solution
into gaseous phase before they are subjected to mass
spectrometric analysis.

macromolecules in solution are forced directly from

the liquid to gas phase. A solution of analytes is passed
through a charged needle that is kept at a high
electrical potential, dispersing the solution into a fine As it is injected into the gas phase, a protein acquires
mist of charged microdroplets. The solvent a variable number of protons, and thus positive
surrounding the macromolecules rapidly evaporates, charges, from the solvent.
leaving multiply charged macromolecular ions in the
gas phase.
 MASS SPECTROMETRY SYNTHESIZED SMALL PEPTIDES & PROTEINS HOW TO
OBTAIN PROTEIN?
Is also used for sequence short stretches of 1. purification from tissue, a task often made difficult
polypeptide, an application that has emerged as an by the vanishingly low concentrations of some
invaluable tool for quickly identifying unknown peptides
proteins 2. genetic engineering
3. direct chemical synthesis.
TANDEM MS OR MS/MS
R. Bruce Merrifield 1962 chemical synthesis of
use of 2 mass spectrometers in tandem peptide
Peptide attached to an insoluble polymer (resin) ex.
Polystyrene bead.

CONSENSUS SEQUENCES

- Is term used for DNA, RNA and protein sequence. - It

is reflected as the most common base or or amino acid
at each position when a series of related nucleic acid
or protein sequences are compared.

SEQUENCE LOGO

- Provides more informative and graphic

representation of an amino acid (or nucleic acid)
multiple sequence alignment than consensus
sequences.

In Biological Process; The same 100 residue protein

would be synthesized with exquisite fidelity in about 5
seconds in a bacterial cell.
 -The logo representation makes the predominance
clear, and a conserved sequence in a protein is made
obvious.

when multiple amino acids are acceptable at a

particular position, they rarely occur with equal
probability. One or few usually predominate.

CHMBIO3 MODULE 1 TRIVIA

1. TITIN
- titin (aka connectin) is the largest known protein and
the longest word in the English language when spelled
out completely

SEQUENCE - titin's name is derived from the Greek word "titan,"

-Each position is separated from its neighbor by a which means "giant”
hyphen. A position where any amino acid is allowed is
designated x. - its full chemical name contains 189,819 letters if
spoken out loud, this word takes over 3 hours to say
-Ambiguities are indicated by listing the acceptable
amino acids for a given position between square helps striated muscles return to their resting length
brackets. For example, in (a) AG means Ala or Gly. after they contract
2. ATPase
-If all but a few amino acids are allowed at one
position, the amino acids that are not allowed are - short for Adenosine Triphosphatase
listed between curly brackets. For example, in (b) W
means any amino acid except Trp. - enzyme responsible for hydrolyzing adenosine
triphosphate (ATP) into adenosine diphosphate (ADP)
- Repetition of an element of the pattern is indicated and inorganic phosphate (Pi)
by following that element with a number or range of
numbers between parentheses. In (a), for example, - has important roles in energy conservation, active
x(4) means x-x-x-x; x(2,4) would mean x-x, or x-x-x, or transport and pH homeostasis
x-x-x-x. 3. LANGUAGE OF LIFE
○ alphabet/letters = amino acids
-A period ends the pattern
○ words = proteins
○ sentences = pathway
○ grammar = DNA
LOGO
○ speaker = cells
-The overall height of the stack (in bits) indicates the
degree of sequence conservation at that position, 4. WHY IS CARBON SO IMPORTANT?
while the height of each symbol in the stack indicates ○ basis of organic chemistry, forming the backbone of
the relative frequency of that amino acid (or countless organic compounds
nucleotide).
○ has four valence electrons, allowing it to form up to
-For amino acid sequences, the colors denote the four bonds with other atoms
characteristics of the amino acid: polar G, S, T, Y, C, Q, ○ its ability to form carbon-carbon (C-C) bonds and
N green; basic K, R, H blue; acidic D, E red; and carbon-hydrogen (C-H) bonds is central to the
hydrophobic A, V, L, I, P, W, F, M black.
structure of biological macromolecules like proteins, ○ For example, some medicines are made up of chiral
nucleic acids (DNA and RNA), carbohydrates, and lipids molecules, and only one of them works as a treatment
while the other might not do anything or even be
○ able to form isomers (molecules with the same harmful. So, scientists need to make sure they use the
chemical formula but different structures) and is correct molecules when designing drugs to help
crucial for the complexity of life people.

○ a fundamental element in the energy-rich molecule ○ Chirality also shows up in nature. For instance, in
adenosine triphosphate (ATP), which serves as the honey, glucose can be left-handed or right-handed.
primary energy currency of cells in living organisms Bees use their enzymes to make only one of them, and
5. WHY IS E.COLI SO IMPORTANT? that's the one we find in honey. So, chirality is like a
hidden feature in the world of tiny molecules, and it
○ Escherichia coli is a type of bacteria commonly found
can have a big impact on our health and the way things
in the intestines of humans and animals
work in nature.
8. DIFFERENTIATE CONFIGURATION,
○ a model organism in biological research due to its
CONFORMATION, AND ECLIPSE.
rapid growth, well-understood genetics, and ease of
○ configuration involves the breaking and forming of
cultivation
chemical bonds
○ has a small genome containing around 4,000 to
○ conformation is the rotation of bonds without
5,000 genes, this simplicity makes it an ideal organism
breaking; reversible; doesn’t form new compounds
for studying basic genetic processes
○ eclipse happens when two adjacent atoms overlap
○ one of the first organisms to have its genome
when viewed along a bond axis; affects the molecule’s
sequenced and is important in our understanding of
stability
the central dogma
9. HOW ARE ENANTIOMERS AND
6. WHY DO WE ARTIFICIALLY MAKE D-AMINO
DIASTEREOMERS DIFFERENT?
ACIDS?
○ both stereoisomers (same formula, same
○ the natural enantiomers for humans are L-amino
connectivity, different arrangement)
acids
○ enantiomers are stereoisomers that are
○ D-amino acids are made so drugs can go to an
nonsuperimposable mirror images; opposite
intended site in the body
configurations at all chirality centers
○ their structure is designed so they would only bind
○ diastereomers are stereoisomers that are non-
to certain receptors and carry out their specific
superimposable non-mirror images; opposite
functions
configurations at some chirality centers
○ in cancer, some of the amino acids appear to be 10. WHY IS THE POLARITY AND CHARGE OF
upregulated, meaning they are in a higher AMINO ACIDS IMPORTANT?
concentration than you would normally find ○ Polarity and charge in amino acids are like magnets
in building blocks. Imagine amino acids as LEGO pieces.
7. WHY IS CHIRALITY A BIG DEAL? Some are magnets (positively or negatively charged),
○ Chirality is like having a pair of shoes, one for your and some have different shapes (polar or nonpolar).
left foot and one for your right foot. They might look When you build something (a protein) with these LEGO
very similar, but they are not the same, and you can't pieces, how they stick together matters a lot.
switch them.
○ In real life, think of making a sandwich. If you put
○ Now, think of molecules as tiny building blocks, and peanut butter (a positively charged amino acid) on one
some of them can be left-handed or right-handed, just slice and jelly (a negatively charged amino acid) on the
like your shoes. In real life, these molecules can have other, they stick together (opposite charges attract).
very different effects in your body.
But if you put two slices of bread (similar amino acids), 15. HOW DO AMINO ACIDS JOIN TOGETHER TO
they don't hold well. FORM PROTEINS?
○ In the first step, the carboxyl group of one amino acid
○ So, in your body, the polarity and charge of amino and the amino group of another come close together.
acids help proteins fold correctly, do their jobs, and
even interact with each other, just like magnets and ○ During condensation, a water molecule (H2O) is
shapes in LEGO help you build cool structures. removed from these groups. One hydrogen atom (-H)
11. WHY IS GLYCINE NOT CHIRAL? from the amino group and one hydroxyl group (-OH)
from the carboxyl group combine to form water.
○ because it lacks a chiral carbon, which is a carbon
atom bonded to four different groups or atoms
○ The remaining parts of the two amino acids, now
with a shared nitrogen-carbon (N-C) bond, create a
○ it has two hydrogen atoms bonded to its central
peptide bond.
carbon, along with an amino group and a carboxyl
group
○ This process continues as more amino acids are
12. WHY IS PROLINE AN IMINO ACID? added, forming a chain of amino acids connected by
○ In most amino acids, the amino group (H3N+) is peptide bonds, which is called a polypeptide.
directly attached to the central carbon atom, forming
an amino acid structure. ○ Finally, polypeptides fold and twist into complex
three-dimensional shapes to become functional
○ However, in proline, the amino group is part of a proteins.
secondary amine called an imino group (H2N+), which 16. HOW CAN YOU EASILY DETERMINE IF AN
is bonded to the central carbon. AMINO ACID IS CHIRAL?
13. WHY IS HISTIDINE CONDITIONALLY ○ A molecule or an amino acid is considered chiral if it
POSITIVELY CHARGED? lacks a plane of symmetry, meaning it cannot be
○ it has an imidazole ring in its side chain, which can superimposed onto its mirror image. To determine
pick up a proton (H+) or lose it depending on the chirality, examine the molecule's structure and look for
surrounding environment's acidity or pH level a central atom, usually carbon, bonded to four
different groups or atoms. If this central atom has four
○ lower pH (acidic) = histidine accepts proton = unique substituents, it is chiral.
positively charged (NH3+)
17. WHAT ARE SOME PRACTICAL APPLICATIONS OF
○ higher pH (basic) = histidine loses proton = CHIRALITY AND ENANTIOMERS IN MEDICINE AND
uncharged (NH2) BIOCHEMISTRY?

○ this ability to switch between charged and ○ In some cases, one enantiomer of a drug may be
uncharged states makes histidine crucial in various effective while the other can be ineffective or even
biological processes including enzyme catalysis, harmful. For instance, the drug Thalidomide had one
protein-protein interactions, and pH regulation enantiomer that caused birth defects and another
14. WHY ARE SOME AMINO ACIDS ESSENTIAL that treated morning sickness. By understanding the
AND NON-ESSENTIAL? differences between enantiomers, researchers can
○ Nine amino acids—histidine, isoleucine, leucine, develop safer and more effective drugs.
lysine, methionine, phenylalanine, threonine,
tryptophan, and valine—are not synthesized by ○ Additionally, the chirality of amino acids and sugars
mammals and are therefore dietarily essential or plays a fundamental role in the structure and function
indispensable nutrients. These are commonly called of biomolecules. Proteins and DNA, for example, rely
the essential amino acids. on specific arrangements of chiral amino acids and
sugars to function correctly, and any alteration in their
○ On the other hand, nonessential amino acids are chirality can disrupt biological processes.
called so because they can be synthesized by the body.