BIOCHEMISTRY

Chapter 2 - Structure and Functions of Biomolecules

A. Proteins

Introduction
This chapter is focused on the structure and functions of biomolecules particularly proteins. Its
subject matter areas such as follows: General properties; Structural Properties; Ionic Properties of amino
acids and the Peptide Bond.

Learning Outcomes:
In this chapter, you are expected to:
1. Describe the general properties of amino acids; and
2. Identify the structural, chemical, and biological properties of the amino acids present in proteins.

Learning Contents:
This chapter contains the following lessons for you to be able to meet the expected learning outcomes:
1. General properties of amino acids and peptides
2. Structural properties of amino acids and peptides
3. Ionic properties of amino acids and peptides
4. The Peptide Bond
For additional information, you can also visit/access the links included under the Recommended learning materials
and resources for supplementary reading part of this chapter.

Teaching and learning Activities:

Each of the lessons in this chapter contains activities that can be done individually, by pair, and by group in an
asynchronous or synchronous mode of learning.

Recommended learning materials and resources for supplementary reading:

The recommended learning materials and resources in this chapter include the URL of the resources from the
Internet (PDF, youtube, slideshare, etc.)

Flexible Teaching Learning Modality (FTLM):

This chapter adopts the synchronous and asynchronous learning modalities for you to have better access and
learning of the lessons. This may include google classroom, moodle, schoology, edmodo, Podcast, printed materials
and other resources depending on your needs and capacity to use the material.

Assessment Task:

At the end of each lesson, you have to answer the given questions for your teacher to check your
understanding. This will help your teacher determine if you need additional explanation and/or activity before
proceeding to the next lesson.
 Chapter 2 A STRUCTURE AND FUNCTIONS OF BIOMOLECULES
(PROTEINS)

JUDY L. RICARDO, MST

Lesson 1
General Properties of Amino Acids

Introduction:
Lesson 1 focused on the general properties of amino acids. All 20 of the common amino
acids are alpha-amino acids. They contain a central C atom, a carboxyl group (COOH), an amino
group (NH2), and a side chain (R group). The R group determines the characteristics (size, polarity,
and pH) for each type of amino acid.

Learning Outcome:
1. Describe the general properties of amino acids;
Learning Contents:

Amino acids are colorless, crystalline solid. Solubility: They are soluble in water, slightly soluble in alcohol and
dissolve with difficulty in methanol, ethanol, and propanol. R-group of amino acids and pH of the solvent play
important role in solubility.

Physical Properties
1. Amino acids are colorless, crystalline solid.
2. All amino acids have a high melting point greater than 200o
3. Solubility: They are soluble in water, slightly soluble in alcohol and dissolve with difficulty in
methanol, ethanol, and propanol. R-group of amino acids and pH of the solvent play important
role in solubility.
4. On heating to high temperatures, they decompose.
5. All amino acids (except glycine) are optically active.
6. Peptide bond formation: Amino acids can connect with a peptide bond involving their amino and
carboxylate groups. A covalent bond formed between the alpha-amino group of one amino acid
and an alpha-carboxyl group of other forming -CO-NH-linkage. Peptide bonds are planar and
partially ionic.

Chemical Properties

1. Zwitterionic property
A zwitterion is a molecule with functional groups, of which at least one has a positive and one has a
negative electrical charge. The net charge of the entire molecule is zero. Amino acids are the best-known
examples of zwitterions. They contain an amine group (basic) and a carboxylic group (acidic). The -
NH2 group is the stronger base, and so it picks up H+ from the -COOH group to leave a zwitterion. The
(neutral) zwitterion is the usual form amino acids exist in solution.

2. Amphoteric property
Amino acids are amphoteric in nature that is they act as both acids and base since due to the two amine and
carboxylic group present.

3. Ionic properties of amino acids• Amino acids contain acidic (COOH) and basic (NH2) groups. Amino
acids are usually ionized at physiologic pH• Therefore, amino acids have amphoteric properties: – In acidic
medium; the amino acid is positively charged, so it behaves as a base (proton acceptor).
Teaching and Learning Activities:
Activity 1. SELF-REFLECTION
Instructions: Following the self-Reflection model (Foronda, 2020) write a 500-word self- reflection about the
general properties of amino acids and the biological importance of amino acids.
Self-reflection model: Reviewing -------- Framing ------- Interpreting, wherein:
1. Reviewing is the first phase in which the students look back to conceptualize and remember
information or ideas;
2. Framing is the second reflective phase where the students create ideas that function to organize
to come up with logical generalization concerning the issues; and
3. Interpreting is the last phase in which students forecast or predict what will happen in the
future concerning the issue.
Recommended learning materials and resources for supplementary reading:
The recommended learning materials and resources in this chapter include the URL of the resources from the
Internet (PDF, youtube, slideshare, etc.)
Assessment Task:

1. Glycine and proline are the most abundant amino acids in the structure of
a) Hemoglobin
b) Myoglobin
c) Insulin
d) Collagen
2. Choose the incorrect statement out of the followings a Only L amino acids are found in the
biological system
a) Glycine is optical inactive
b) Tyrosine is a modified amino acid
c) Seleno cysteine is 21st amino acid
3Which out of the following amino acids carries a net positive charge at the physiological pH
a) Valine
b) Leucine
c) Isoleucine
d) None of the followings
4Which out of the following amino acids is a precursor for a mediator of allergies and
inflammation?
a) Histidine
b) Tyrosine
c) Phenyl Alanine
d) Tryptophan
5All of the below mentioned amino acids can participate in hydrogen bonding except one
a) Serine
b) Cysteine
c) Threonine
d) Valine
 Chapter 2 A STRUCTURE AND FUNCTIONS OF BIOMOLECULES
(PROTEINS)

Lesson 2
Structural Properties of Amino Acids

Introduction:
The structure of an amino acid allows it to act as both an acid and a base. An amino acid has this ability
because at a certain pH value (different for each amino acid) nearly all the amino acid molecules exist as zwitterions.

Learning Outcome:
1. Describe the structure of an amino acid and the features that confer its specific
properties.
Learning Content:

Structure of an Amino Acid

Amino acids are the monomers that make up proteins. Each amino acid has the same fundamental structure,
which consists of a central carbon atom, also known as the alpha (α) carbon, bonded to an amino group
(NH2), a carboxyl group (COOH), and to a hydrogen atom. In the aqueous environment of the cell, the both
the amino group and the carboxyl group are ionized under physiological conditions, and so have the
structures -NH3+ and -COO–, respectively. Every amino acid also has another atom or group of atoms
bonded to the central atom known as the R group. This R group, or side chain, gives each amino acid
proteins specific characteristics, including size, polarity, and pH.

Amino acid structure

Amino acids have a central asymmetric carbon to which an amino group, a carboxyl group, a hydrogen
atom, and a side chain (R group) are attached. This amino acid is unionized, but if it were placed in water at
pH 7, its amino group would pick up another hydrogen and a positive charge, and the hydroxyl in its
carboxyl group would lose and a hydrogen and gain a negative charge.
Types of Amino Acids
The name “amino acid” is derived from the amino group and carboxyl-acid-group in their basic
structure. There are 21 amino acids present in proteins, each with a specific R group or side chain. Ten of
these are considered essential amino acids in humans because the human body cannot produce them and
they must be obtained from the diet. All organisms have different essential amino acids based on their
physiology.
The 20 amino acids of proteins are often referred to as the standard, primary, or normal amino acids,
to distinguish them from amino acids within proteins that are modified after the proteins are synthesized,
and from many other kinds of amino acids present in living organisms but not in proteins. The standard
amino acids have been assigned three-letter abbreviations and one-letter symbols which are used as
shorthand to
Table 1. the 20 amino acids and their 3-letter /1-letter abbreviation

We note in the figure 5-2 below, that for all the standard amino acids except one (glycine) that the
alpha carbon is asymmetric, bonded to four different substituent groups: a carboxyl group, an amino group,
an R group, and a hydrogen atom. The alpha-carbon atom is thus chiral center see figure 5-2. Because of the
tetrahedral arrangement of the bonding orbitals around the a-carbon atom of amino acids, the four different
substituent groups can occupy two different arrangements in space which are nonsuperimposable mirror
images of each other (see figure 3-9).
 Figure 3-9
b) When there are only three dissimilar groups
around the carbon atom (i.e. the same group
occurs twice), only one configuration in space is
a) When a carbon atom has four possible and the molecule is asymmetric, or
different substituent groups (A, B, achiral. In this case the molecule is
X, Y) they can be arranged in two superimposable on its mirror image: the
ways that represent molecule on the left can be rotated
nonsuperimposable mirror images counterclockwise (when looking down its
of each other (enantiomers). Such vertical bond from A to C to create the
a carbon atom is asymmetric and molecule on the right
is called a chiral atom or chiral
center.

These two forms are called enantiomers or stereoisomers see figure 5- 2. All molecules with a chiral
center are also optically active. Ex. They can rotate plane-polarized light, with the direction of the rotation
differing for different stereoisomers.
The classification and naming of stereoisomers is based on the absolute configuration of the four
substituents of the asymmetric carbon atom. For this purpose, a reference compound has been chosen to
which all other optically active compounds are compared. This reference compound is the 3-carbon sugar
glyceraldehyde (see figure 5-4 below) the smallest sugar to have an asymmetric carbon atom. The naming of
configurations of both simple sugars and amino acids is based on the absolute configuration of
glyceraldehyde, as established by x-ray diffraction analysis. The stereoisomers of all chiral compounds
having a configuration related to that of L-glyceraldehyde are designated L (for levorotatory, derived from
levo, meaning left, and the stereoisomers related to D-glyceraldehyde are designated D for dextrorotatory,
derived from dextro, meaning right. The symbols L and D thus refer to the absolute configuration of the four
substituents around the chiral carbon.

PROTEINS CONTAIN L-AMINO ACIDS

Nearly all biological compounds with a chiral center occur naturally in only one stereoisomeric form,
either D or L. the amino acids in protein molecules are the L stereoisomers. D-Amino acids have been found
only in small peptides of bacterial cell walls and in some peptide antibiotics see figure 5-19.
 It is remarkable that the amino acids of proteins are all L stereoisomers. When chiral compounds are
formed by ordinary chemical reactions, a racemic mixture of D and L isomers results. Whereas the L and D
forms of chiral molecules are difficult for a chemist to distinguish and isolate, they are as different as night
and day to a living system.
Amino acids can be classified by R Group
The amino acids are grouped into classes based on the properties of their R groups in particular, their
polarity or tendency to interact with water at biological pH (near pH 7.0). the polarity of the R groups varies
widely, from totally nonpolar or hydrophobic (water-insoluble) to highly polar or hydrophilic (water-
soluble).
The structures of the 20 standard amino acids are shown in figure below
 There are five main classes of amino acids, those whose R groups are: nonpolar and aliphatic;
aromatic (generally nonpolar); polar but uncharged; negatively charged; and positively charged. Within each
class there are gradations of polarity, size, and shape of the R groups.

NONPOLAR, ALIPHATIC R GROUPS

The hydrocarbon R groups in this class of amino acids are nonpolar and hydrophobic. The bulky
side chains of alanine, valine, leucine, and isoleucine, with their distinctive shapes, are important in
promoting hydrophobic interactions within protein structures. Glycine has the simplest amino acid structure.
where it is present in a protein, the minimal steric hindrance of the glycine side chain allows much more
structural flexibility than the other amino acids. Proline represents the opposite structural extreme. The
secondary amino (imino) group is held in a rigid conformation that reduces the structural flexibility of the
protein at that point.

AROMTIC R GROPUS PHENYLALANINE, TYROSINE, AND TRYPTOPHAN

With their aromatic side chains are relatively nonpolar (hydrophobic). All can participate in hydrophobic
interactions, which are particularly strong when the aromatic groups are stacked on one another. The
hydroxyl group of tyrosine can form hydrogen bonds, and it acts as an important functional group in the
activity of some enzymes. Tyrosine and tryptophan are significantly more polar than phenylalanine-nine
because of the tyrosine hydroxyl group and the nitrogen of the tryptophan indole ring.

POLAR, UNCHARGED R GROUPS

 The R groups of these amino acids are more soluble in water or hydrophilic than those of the
nonpolar amino acids, because they contain functional groups that form hydrogen bonds with water. This
class of amino acids includes serine, threonine, cystine, methionine, asparagine, and glutamine. The
polarity of serine and threonine is contributed by their hydroxyl groups; that of cystine and methionine by
their sulfur atom; and that of asparagine and glutamine by their amide groups.
Asparagine and glutamine are the amides of two other amino acids also found in proteins, aspartate
and glutamate respectively to which asparagine and glutamine are easily hydrolyzed by acid or base.
Cysteine has an R group (a thiol group) that is approximately as acidic as the hydroxyl group of tyrosine.
Cysteine requires special mention for another reason. It is readily oxidized to form a covalently linked
dimeric amino acid called cystine, in which two cysteine molecules are joined by a disulfide bridge.
Disulfide bridges of this kind occur in many proteins, stabilizing their structures.

NEGATIVELY CHARGED (ACIDIC) R GROUPS

The two amino acids having R groups with a net negative charge at pH 7.0 are aspartate and
glutamate, each with a second carboxyl group. These amino acids are the parent compounds of asparagine
and glutamine respectively.

POSITIVELY CHARGED (BASIC) R GROUPS

The amino acids in which the R groups have a net positive charge at pH 7.0 are lysine, which has a
second amino group at the position on its aliphatic chain; arginine, which has a positively charged
guanidino group; and histidine, containing an imidazole group. Histidine is the only standard amino acid
having a side chain with a pKa near neutrality.

Types of amino acids

There are 21 common amino acids commonly found in proteins, each with a different R group
(variant group) that determines its chemical nature. The 21st amino acid, not shown here, is
selenocysteine, with an R group of -CH2-SeH.

Characteristics of Amino Acids

 Which categories of amino acid would you expect to find on the surface of a soluble protein, and
which would you expect to find in the interior? What distribution of amino acids would you expect
to find in a protein embedded in a lipid bilayer?
 The chemical composition of the side chain determines the characteristics of the amino acid. Amino
acids such as valine, methionine, and alanine are nonpolar (hydrophobic), while amino acids such as
serine, threonine, and cysteine are polar (hydrophilic). The side chains of lysine and arginine are
positively charged so these amino acids are also known as basic (high pH) amino acids. Proline is an
exception to the standard structure of an amino acid because its R group is linked to the amino group,
forming a ring-like structure.
 Amino acids are represented by a single upper-case letter or a three-letter abbreviation. For example,
valine is known by the letter V or the three-letter symbol val.

Classification of amino acids on the basis of R-group

1. Nonpolar, Aliphatic amino acids: The R groups in this class of amino acids are nonpolar and
hydrophobic. Glycine, Alanine, Valine, leucine, Isoleucine, Methionine, Proline.
2. Aromatic amino acids: Phenylalanine, tyrosine, and tryptophan, with their aromatic side chains, are
relatively nonpolar (hydrophobic). All can participate in hydrophobic interactions.
3. Polar, Uncharged amino acids: The R groups of these amino acids are more soluble in water, or
more hydrophilic, than those of the nonpolar amino acids, because they contain functional groups
 that form hydrogen bonds with water. This class of amino acids includes serine, threonine, cysteine,
asparagine, and glutamine.
4. Acidic amino acids: Amino acids in which R-group is acidic or negatively charged. Glutamic acid
and Aspartic acid
5. Basic amino acids: Amino acids in which R-group is basic or positively charged. Lysine, Arginine,
Histidine
Classification of amino acids on the basis of nutrition
1. Essential amino acids (Nine)
Nine amino acids cannot be synthesized in the body and, therefore, must be present in the diet in order for
protein synthesis to occur.
These essential amino acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine.
2. Non-essential amino acids (Eleven)
These amino acids can be synthesized in the body itself and hence not necessarily need to be acquired
through diet.
Arginine, glutamine, tyrosine, cysteine, glycine, proline, serine, ornithine, alanine, asparagine, and aspartate.
3. Conditionally

Classification of amino acids on the basis of the metabolic fate

1. Glucogenic amino acids: These amino acids serve as precursors gluconeogenesis for glucose
formation. Glycine, alanine, serine, aspartic acid, asparagine, glutamic acid, glutamine, proline,
valine, methionine, cysteine, histidine, and arginine.
2. Ketogenic amino acids: These amino acids breakdown to form ketone bodies. Leucine and Lysine.
3. Both glucogenic and ketogenic amino acids: These amino acids breakdown to form precursors for
both ketone bodies and glucose. Isoleucine, Phenylalanine, Tryptophan, and tyrosine.
Functions of Amino acids
1. 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.
2. The linear sequence of amino acid residues in a polypeptide chain determines the three-dimensional
configuration of a protein, and the structure of a protein determines its function.
3. 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
• The health of vital organs
• Normal cellular structure
4. The amino acids are used by various tissues to synthesize proteins and to produce nitrogen-
containing compounds (e.g., purines, heme, creatine, epinephrine), or they are oxidized to produce
energy.
5. The breakdown of both dietary and tissue proteins yields nitrogen-containing substrates and carbon
skeletons.
6. The nitrogen-containing substrates are used in the biosynthesis of purines, pyrimidines,
neurotransmitters, hormones, porphyrins, and nonessential amino acids.
7. The carbon skeletons are used as a fuel source in the citric acid cycle, used for gluconeogenesis, or
used in fatty acid synthesis.

Teaching and Learning Activities:

Activity 1.
a. Draw the structure for the anion formed when glycine (at neutral pH) reacts with a base.

b. Draw the structure for the cation formed when glycine (at neutral pH) reacts with an acid.
Recommended learning materials and resources for supplementary reading:
The recommended learning materials and resources in this chapter include the URL of the resources from the
Internet (PDF, youtube, slideshare, etc.)
Assessment Task:

MULTIPLE CHOICE:
1. Identify the amino acids containing nonpolar, aliphatic R groups.

a. Phenylalanine, tyrosine, and tryptophan

b. Glycine, Alanine, Leucine
c. Lysine, Arginine, Histidine
d. Serine, Threonine, Cysteine

2. The two amino acids having R groups with a negative net charge at pH 7.0 are _______
a. Aspartate, and Glutamate
b. Arginine and Histidine
c. Cysteine and Methionine
d. Proline and Valine
[Link] of the following is a non- essential amino acid?
a. Serine
b. Threonine
c. Lysine
d. Histadine
4. Which of the following is an essential amino acid?
a. Cystine
b. Asparagine
c. Glutamine
d. Phenylalanine
5. Which of the following is an imino acid?
a. Alanine
b. Glycine
c. Proline
d. Serine
6. How many numbers of chiral centers are there in Isoleucine?
a. 1
b. 2
c. 3
d. 4

Chapter 2 A STRUCTURE AND FUNCTIONS OF BIOMOLECULES

(PROTEINS)

Lesson 3
The Peptide Bond

Introduction:
We now turn to polymers of amino acids, the peptides. Biologically occurring peptides range in size
from small molecules containing only two or three amino acids to macromolecules containing thousands of
amino acids. The focus here is on the structure and chemical properties of the smaller peptides, providing a
prelude to the discussion of the large peptides called proteins.
Learning Outcome:
1. identify the amino acids that joined by peptide bonds.
Learning Contents:

Peptide Bonds

The sequence and the number of amino acids ultimately determine the protein’s shape, size, and
function. Each amino acid is attached to another amino acid by a covalent bond, known as a peptide bond.
When two amino acids are covalently attached by a peptide bond, the carboxyl group of one amino acid and
the amino group of the incoming amino acid combine and release a molecule of water. Any reaction that
combines two monomers in a reaction that generates H 2O as one of the products is known as a dehydration
reaction, so peptide bond formation is an example of a dehydration reaction.

Peptide bond formation

Peptide bond formation is a dehydration synthesis reaction. The carboxyl group of one amino acid is
linked to the amino group of the incoming amino acid. In the process, a molecule of water is released.

Three amino acids can be joined by two peptide bonds to form a tripeptide; similarly, amino acids
can be linked to form tetrapeptides and pentapeptides. When a few amino acids are joined in this fashion.
The structure is called an oligopeptide. When many amino acids are joined, the product is called a
polypeptide.
Proteins may have thousands of amino acids units. Although the term protein and polypeptide are sometimes
used interchangeably, molecules referred to as polypeptides generally have molecular weights below 10,000.

Figure 5-16 shows the structure of a pentapeptide.

 The amino acid units in a peptide are often called residues (each has lost a hydrogen atom from its
amino group and a hydroxyl moiety from its carboxyl group). The amino acid residue at that end of a
peptide having a free a-amino group is the amino-terminal (or N-terminal) residue; the residue at the other
end, which has a free carboxyl group, is the carboxyl-terminal (C-terminal) residue. By convention, short
peptides are named from the sequence of their constituent amino acids, beginning at the left with the amino-
terminal residue and proceeding toward the carboxyl terminus at the right.
Although hydrolysis of peptide bonds is an exergonic reaction, it occurs slowly because of its high
activation energy. As a result, the peptide bonds in proteins are quite stable under most intracellular
conditions.
The peptide bond is the single most important covalent bond linking amino acids in peptides and
proteins. The only other type of covalent bond that occurs frequently enough to deserve special mention here
is the disulfide bond sometimes formed between two cysteine residues. Disulfide bonds play a special role in
the structure of many proteins, particularly those that function extracellularly, such as the hormone insulin
and the immunoglobulins or antibodies.

PEPTIDES CAN BE DISTINGUISHED BY THEIR IONIZATION BEHAVIOR

Peptides contain only one free alpha-amino group and one free alpha-carboxyl group. (Figure 5-17).
 These groups ionize as they do in simple amino acids, although the ionization constants are different
because the oppositely charged group is absent from the alpha carbon. The alpha-amino and alpha-carboxyl
groups of all other constituent amino acids are covalently joined in the form of peptide bonds, which do not
ionize and thus do not contribute to the total acid-base behavior of peptides. However, the R groups of some
amino acids can ionize and, in a peptide, these contribute to the overall acid-base properties. Figure 5-17.
Thus, the acid-base behavior of a peptide can be predicted from its single free alpha amino and alpha-
carboxyl groups and the nature and number of its ionizable R groups. Like free amino acids, peptides have
characteristic titration curves and a characteristic isoelectric pH at which they do not move in an electric
field. These properties are exploited in some of the techniques used to separate peptides and proteins.

PEPTIDES UNDERGO CHARACTERISTIC CHEMICAL REACTIONS

Like other organic molecules, peptides undergo chemical reactions that are characteristic of their
functional groups: the free amino and carboxyl groups and the R groups.
Peptide bonds can be hydrolyzed by boiling with either strong acid typically 6 m HCl or base to yield
the constituent amino acids.
 Hydrolysis of peptide bonds in this manner is a necessary step in determining the amino acid
composition of proteins. The reagents shown in figure 5-14 label only free amino groups: those of the
amino-terminal residue and the R groups of any lysines present. If dabsyl chloride, dansyl chloride, or 1-
fluoro-2,4-dinitrobenzene is used before acid hydrolysis of the peptide, the amino-terminal residue can be
separated and identified figure 5-18.
 Peptide bonds can be hydrolyzed by certain enzymes called proteases. Proteolytic (protein-cleaving)
enzymes are found in all cells and tissues, where they degrade unneeded or damaged proteins or aid in the
digestion of food.

SOME SMALL POLYPEPTIDES HAVE BIOLOGICAL ACTIVITY

Not all polypeptides are so large, however there are many naturally occurring small poplypeptides
and oligopeptides, some of which have important biological activities and exert their effects at very low
concentrations. For example, a number of vertebrate hormones (intercellular chemical messengers) are small
polypeptrides. The hormone insulin contains two polypeptide chains, one having 30 amino acid residues and
the other 21. Other polypeptide hormones include glucagon, a pancreatic hormone of 29 residues that
opposes the action of insulin, and corticotropin, a 39-residue hormone of the anterior pituitary gland that
stimulates the adrenal cortex.

Polypeptide Chains

The resulting chain of amino acids is called a polypeptide chain. Each polypeptide has a free amino
group at one end. This end is called the N terminal, or the amino terminal, and the other end has a free
carboxyl group, also known as the C or carboxyl terminal. When reading or reporting the amino acid
sequence of a protein or polypeptide, the convention is to use the N-to-C direction. That is, the first amino
acid in the sequence is assumed to the be one at the N terminal and the last amino acid is assumed to be the
one at the C terminal.

Although the terms polypeptide and protein are sometimes used interchangeably, a polypeptide is
technically any polymer of amino acids, whereas the term protein is used for a polypeptide or polypeptides
that have folded properly, combined with any additional components needed for proper functioning, and is
now functional.

Teaching and Learning Activities:

Activity 1.
Naming the Stereoisomers of Isoleucine. The structure of the amino acid isoleucine is:
 COO-

H3N – C – H

H - C – CH3

CH2

CH3

1. How many chiral centers does it have?

2. How many optical isomers?
3. Draw perspective formulas for all the optical isomers of isoleucine.

Recommended learning materials and resources for supplementary reading:

The recommended learning materials and resources in this chapter include the URL of the resources from the
Internet (PDF, youtube, slideshare, etc.)

Flexible Teaching Learning Modality (FTLM):

This chapter adopts the synchronous and asynchronous learning modalities for you to have better access and
learning of the lessons. This may include google classroom, moodle, schoology, edmodo, Podcast, printed materials
and other resources depending on your needs and capacity to use the material.

Assessment Task:

MULTIPLE CHOICE:
1. Peptide bond is a __________
a. Covalent bond
b. Ionic bond
c. Metallic bond
d. Hydrogen bond

2. A tripeptide has _____________

a. 3 amino acids and 1 peptide bond
b. 3 amino acids and 2 peptide bonds
c. 3 amino acids and 3 peptide bonds
d. 3 amino acids and 4 peptide bonds
3. Which of the following is a 39- residue hormones of the anterior pituitary gland?
a. Carticotropine
b. Glucagon
c. Insulin
d. Bradykinin