Phorutai Pearngam (Pear)

[email protected]
Academic year, 2023-2024
Overview of today’s lecture
❑ Carbohydrate
❑ Lipid
❑ Protein
❑ Nucleic acids
Nucleotides

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Overview: The Molecules of Life
▪ All living things made up of four classes of large biological molecules, macromolecules
• Macromolecules are large molecules composed of thousands of covalently
connected atoms
• Molecular structure and function are inseparable Lipid= wot polymer
▪ Macromolecules are polymers, built from monomers
▪ A polymer long molecule consisting of many similar building blocks
▪ These small building-block molecules are called monomers
▪ Three of four macromolecule classes are polymers
▪ Carbohydrates, Proteins, Nucleic acids, Not lipids
▪ Each cell has thousands of different macromolecules among cells of an organism, within
a species, even more between species
▪ An immense variety of polymers from a small set of monomers

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Synthesis and Breakdown of Polymers
▪ Dehydration reaction: two monomers bond
together through ‘lost’ of a water molecule

▪ Hydrolysis: breaks down polymers to monomers

by ‘addition’ of water, which breaks bond in
monomer chain (essentially reverse of
dehydration reaction)

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Carbohydrates: Fuel and building material

▪ Carbohydrates include sugars and polymers of sugars

▪ Monosaccharides: The simplest carbohydrates or simple sugars
▪ Disaccharides: Double sugars, consisting of two monosaccharides joined by
a covalent bond
▪ Polysaccharides: Carbohydrate composed of many sugar building blocks

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Sugars: Monosaccharides
▪ Monosaccharides have molecular formulas that are usually multiples of
the unit CH2O (C:H:O = 1:2:1)
▪ Glucose (C6H12O6) is most common monosaccharide
▪ The trademarks of a monosaccharide:
• A carbonyl group Ier
• Multiple hydroxyl groups —OH
▪ Monosaccharide diversity can be classified by some criteria
• Depending on the location of the carbonyl group, a monosaccharide
is either an aldose (aldehyde sugar) or a ketose (ketone sugar)
• The size of the carbon skeleton, which ranges from three to seven
carbons long
• The way their parts are arranged spatially around asymmetric
carbons, see glucose and galactose

https://opentextbc.ca/chemistry/chapter/20-3-
aldehydes-ketones-carboxylic-acids-and-esters/
Sugars: Monosaccharides
▪ In aqueous solutions, glucose molecules, as well as most other five- and six-carbon
sugars, form rings, because they are the most stable form

▪ Monosaccharides serve as a major fuel for cells and as raw material for building
molecules
▪ Monosaccharides that are not immediately used are generally incorporated as
monomers into disaccharides or polysaccharides
Sugars: Disaccharide
▪ A disaccharide is formed when a dehydration reaction joins two monosaccharides by the
covalent bond called a glycosidic linkage
▪ Three common examples are sucrose (Glu+Fruc), lactose (Glu+Galac), and maltose
(Glu+Glu)

dehydration
=
Sugars: Disaccharide
▪ Disaccharides must be broken down into monosaccharides to be used for energy by
organisms
▪ Lactose intolerance is a common condition in humans who lack lactase, the enzyme that
breaks down lactose
▪ A lactose molecule is instead broken down by intestinal bacteria, causing formation of
gas and subsequent cramping

https://www.foodbusinessnews.net/
Polysaccharide
▪ Polymers with a few hundred to a few thousand monosaccharides joined by glycosidic
linkages
▪ Polysaccharide can be characterised by their roles:
• Storage materials: hydrolysation provides monosaccharides for cells
• Structural material: building material for structures that protect the cell or organism
▪ The architecture and function of a polysaccharide are determined by...
• Its monosaccharides
• The positions of its glycosidic linkages
Storage Polysaccharides
▪ Starch: store sugars for later use in the form of storage polysaccharides of plants
• Consists entirely of glucose monomers, joined by 1–4 linkages
• Plants store surplus starch as granules within chloroplasts and other plastids
• Potato tubers and grains—the fruits of wheat, corn, rice, and other grasses—are the major
sources of starch for human diets
• Amylose is the simplest form, unbranched
• Amylopectin is more complex, a branched polymer with 1–6 linkages at the branch points
Storage Polysaccharides
▪ Glycogen: a storage polysaccharide in animals
• Vertebrates store glycogen mainly in liver and muscle cells
• Breakdown of glycogen in these cells releases glucose when the demand for energy
increases
• The structure is like amylopectin but more extensively branched
▪ The extensively branched structure of glycogen allows more free
ends are available for breakdown providing a glucose for
metabolism process faster rate
Structural Polysaccharides
▪ Cellulose: major component of tough cell wall of plant cells
• A polymer of glucose with 1–4 glycosidic linkages
• There are two slightly different ring structures for glucose, which are α and β
configuration
• That difference makes cellulose is unlike starch
• There are α glucoses in starch, but they are β configuration in cellulose, making
every glucose monomer “upside down” respect to its neighbor
α glucose β glucose
Structural Polysaccharides
▪ Cellulose: major component of tough cell wall of plant cells
• The structure is straight, never branched, and some hydroxyl groups on its monomers are
free to form hydrogen-bond with the lying parallel cellulose molecules
• The parallel celluloses held together can form structural units called microfibrils
• Enzymes that digest starch by hydrolyzing α linkages can’t hydrolyze β linkages in cellulose
• Cellulose in human food therefore passes through digestive tract as insoluble fiber
• Some microbes use enzymes to digest cellulose
• Many herbivores, from cows to termites, have symbiotic relationships with microbes who
have enzymes to digest cellulose
Structural Polysaccharides
▪ Chitin: the carbohydrate used by arthropods
• Arthropods include insects, spiders, crustaceans, and related animals
• These animal use chitin to build their exoskeletons (hard cases that surround the soft
parts of an animal)
• The structure is similar to cellulose, with β linkages, except that the glucose monomer of
chitin has a nitrogen-containing attachment
Lipids: A diverse group of hydrophobic molecules
▪ Lipids do not form polymers
▪ Unifying feature of lipids: little or no affinity for water (hydrophobic)
▪ Hydrophobic because consist mostly of hydrocarbons which form nonpolar covalent
bonds (non-polar C—H bonds)
▪ Most biologically important lipids are fats, phospholipids, and steroids

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Fats
▪ Large molecules assembled from smaller molecules by dehydration reactions
▪ A fat consists of a glycerol molecule joined to three fatty acids
▪ Glycerol is an alcohol; each of its three carbons bears a hydroxyl group
▪ A fatty acid has a long carbon skeleton (16 or 18 atoms) attached with a carboxyl group
carboxyl group
Hydroxyl group

▪ Fats separate from water because the water molecules form hydrogen
bonds to each other and exclude the fats
Fats
▪ The completed fat consists of three fatty acids linked to one glycerol molecule
▪ Each fatty acid molecule is joined to glycerol by a dehydration reaction, which forms an
ester linkage, a bond between a hydroxyl group and a carboxyl group

Other names for a fat are

triacylglycerol and triglyceride

▪ Based on the difference of structure of the hydrocarbon chains , the fatty acids can be
divided in two to types, which are saturated fats and unsaturated fats
Fats
▪ Saturated fats: Animal fats, such as lard and butter
• Saturated fatty acids have no double bond, so the number of hydrogen atoms in
carbon chain can be as many as possible
• Solid at room temperature because the flexibility allows the fat molecules to pack
together tightly
Fats
▪ Unsaturated fats: The fats of plants and fishes,
so-called oils
▪ Unsaturated fatty acids have one or more
double bonds, so carbon atoms on each
double-bonded carbon have one fewer
hydrogen
▪ A cis double bond can create a kink in the
hydrocarbon chain
▪ Liquid at room temperature since the kinks
prevent the molecules from tight packing

- >is

- trans
Fats
▪ A diet rich in saturated fats may contribute to cardiovascular
disease through plaque deposits
▪ Hydrogenation is process of converting unsaturated fats to
saturated fats by adding hydrogen
https://www.medicinenet.com/whats_at
▪ The process of hydrogenating vegetable oils produces trans herosclerosis/article.htm

fats, unsaturated fats with trans double bonds

▪ Trans fats may contribute more than saturated fats to
cardiovascular disease

https://www.eleatnutrition.com/blog/nut-butters
Fats
▪ The major function of fats is energy storage
▪ Humans and other mammals store fat in adipose cells
▪ Adipose tissue also cushions vital organs and insulates body

Blausen.com staff (2014)

Phospholipids
▪ In phospholipid, two fatty acids and phosphate group are attached to glycerol
▪ Two fatty acid tails are hydrophobic, but phosphate group and its attachments are
hydrophilic head
▪ When phospholipids are added to water, they self-
assemble into a bilayer, with the hydrophobic tails
pointing toward the interior
▪ The structure of phospholipids results in a bilayer
arrangement found in cell membranes
Steroids
▪ Steroids are lipids characterized by a carbon skeleton consisting of four fused rings
▪ Cholesterol, an important steroid, is a component in animal cell membranes
▪ Although cholesterol is essential in animals, high levels in the blood may contribute to
cardiovascular disease

Cholesterol is the molecule from which other steroids,

including the sex hormones, are synthesized. Steroids
vary in the chemical groups attached to their four
interconnected rings
Protein: A biologically functional molecule
▪ Proteins account for more than 50% of dry mass of most cells
▪ Protein functions include support, storage, transport, communications, movement, and
immunity

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Protein: A biologically functional molecule
▪ Enzymes are a type of protein that acts as a catalyst to speed up chemical reactions
▪ Enzymes can perform their functions repeatedly, functioning as workhorses that carry out
the processes of life

https://www.genome.gov/genetics-glossary/Enzyme 26
Protein: A biologically functional molecule
▪ Proteins are all constructed from the same set of 20
amino acids
▪ The bond between amino acids is called a peptide
bond, so a polymer of amino acids is called a
polypeptide.
▪ A protein is a biologically functional molecule made up
of one or more polypeptides
▪ Each folded and coiled into a specific three-dimensional
structure that refer to a specific function of the protein
▪ The vast variety in structure contributes to high
diversity of function

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Amino Acids (Monomers)
▪ Amino acids are organic molecules with carboxyl and amino groups
▪ Amino acids differ in their properties due to differing side chains,
called R groups
▪ At the center of the amino acid is an asymmetric carbon atom
called the alpha (α) carbon
▪ The physical and chemical properties of the side chain determine
the unique characteristics of a particular amino acid
 The non-ionized and ionized forms of a generic amino acid

The specific amino acids are shown below in their ionized

form, prevalent at the pH within a cell (pH 7.2). The amino
acids are grouped by properties of their side chains. The
three-letter and one-letter abbreviations for the amino
acids are in parentheses.
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Polypeptides (Amino Acid Polymers)
▪ A polypeptide is a polymer of amino acids joined by
a dehydration reaction resulting to forming a
peptide bond
▪ Polypeptides range in length from a few to more
than a thousand monomers
▪ Each polypeptide has a unique linear sequence of
amino acids, with a carboxyl end (C-terminus) and
an amino end (N-terminus)
Protein Structure and Function
▪ A functional protein is not just a polypeptide chain, but one or more polypeptides
precisely twisted, folded, and coiled into a molecule of unique shape
Protein Structure and Function
▪ The sequence of amino acids determines a protein’s three-dimensional structure
▪ A protein’s structure determines its function
Four Levels of Protein Structure
▪ The primary structure of a protein is its unique Primary
sequence of amino acids
▪ Secondary structure, found in most proteins, consists
of coils and folds in the polypeptide chain
▪ Tertiary structure is determined by interactions Secondary
among various side chains (R groups)
▪ Quaternary structure results when a protein consists
of multiple polypeptide chains
Tertiary

Quaternary
Primary structure
▪ The sequence of amino acids in a protein, is like the
order of letters in a long word
▪ Primary structure is determined by inherited genetic
information
Sickle-Cell Disease: A Change in Primary Structure
▪ A slight change in primary structure can affect a protein’s structure and ability to function
▪ Sickle-cell disease, an inherited blood disorder, results from a single amino acid
substitution in the protein hemoglobin
Secondary structure
▪ The coils and folds of secondary structure result from hydrogen bonds between repeating
constituents of the polypeptide backbone
▪ Typical secondary structures are a coil called an α helix and a folded structure called a β
pleated sheet

Spiders secrete silk fibers made of a

structural protein containing β pleated
sheets, which allow the spiderweb to
stretch and recoil
Tertiary structure
▪ The overall shape of a polypeptide resulting from interactions between the side chains (R
groups) of the various amino acids
▪ These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic
interactions, and van der Waals interactions
▪ Strong covalent bonds called disulfide bridges (can form where two cysteine monomers)
may reinforce the protein’s structure
Quaternary structure
▪ Two or more polypeptide subunits form one macromolecule
▪ For example…
▪ Collagen is a fibrous protein consisting of three polypeptides coiled like a rope

▪ Hemoglobin is a globular protein consisting

of four polypeptides: two alpha and two beta
chains
What Determines Protein Structure?
▪ In addition to primary structure, physical and chemical conditions can affect structure
▪ Alterations in pH, salt concentration, temperature, or other environmental factors can
cause a protein to unravel
▪ This loss of a protein’s native structure is called denaturation
▪ A denatured protein is biologically inactive

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Protein Folding in the Cell
▪ It is hard to predict a protein’s structure from its primary structure
▪ Most proteins probably go through several stages on their way to a stable structure
▪ Chaperonins are protein molecules that assist the proper folding of other proteins
▪ Diseases such as Alzheimer’s, Parkinson’s, and mad cow disease are associated with
misfolded proteins
Protein structure determining
▪ Scientists use X-ray crystallography to determine a protein’s structure
▪ Another method is nuclear magnetic resonance (NMR) spectroscopy, which does not
require protein crystallization
▪ Bioinformatics uses computer programs to predict protein structure from amino acid
sequences

X-ray crystallography

Electron Density map

Nucleic acids: A function molecules for hereditary information
▪ The amino acid sequence of a polypeptide is
programmed by a unit of inheritance called a gene
▪ Genes are made of DNA, a nucleic acid made of
monomers called nucleotides
▪ Gene expression is the process raising by the roles
of nucleic acids
• There are two types of nucleic acids including
Deoxyribonucleic acid (DNA) and Ribonucleic
acid (RNA)
• DNA provides directions for its own replication
• DNA directs synthesis of messenger RNA (mRNA)
and, through mRNA, controls protein synthesis
• Protein synthesis occurs on ribosomes
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The Components of Nucleic Acids
▪ Nucleic acids are polymers called polynucleotides
▪ Each polynucleotide is made of monomers called nucleotides
▪ Adjacent nucleotides are joined by covalent bonds that
form between the —OH group on the 3′ carbon of one
nucleotide and the phosphate on the 5′ carbon on the
next

▪ These links create a backbone of sugar-phosphate units

with nitrogenous bases as appendages
The Components of Nucleic Acids

▪ Each nucleotide consists of a nitrogenous base, a pentose sugar, and one or more phosphate groups
▪ The portion of a nucleotide without the phosphate group is called a nucleoside
▪ There are two families of nitrogenous bases
▪ Pyrimidines (cytosine (C), thymine (T), and uracil (U)) have a single six-
membered ring
▪ Purines (adenine (A) and guanine (G)) have a six-membered ring fused to a
five-membered ring
▪ In DNA, the sugar is deoxyribose; in RNA, the sugar is ribose Nucleoside = nitrogenous
base + sugar

▪ The sequence of bases along a DNA or mRNA

polymer is unique for each gene

Nucleotide = nucleoside + phosphate group

The Structures of DNA and RNA Molecules
▪ RNA molecules usually exist as single polypeptide chains
▪ DNA molecules have two polynucleotides spiraling around an imaginary axis, forming a double helix
▪ In the DNA double helix, the two backbones run in opposite 5′→ 3′ directions from each other, an
arrangement referred to as antiparallel
▪ The nitrogenous bases in DNA pair up and form
hydrogen bonds: A and T pair, G and C pair, called
complementary base pairing
▪ Complementary pairing can also occur between two
RNA molecules or between parts of the same
molecule such as transfer RNA (tRNA)
▪ In RNA, thymine is replaced by uracil (U) so A and U
pair