OVERVIEW: PREVIOUS LECTURE (L4)
❑ Define the endomembrane system?
❑ Which organelles form part of the endomembrane
system?
❑ What are each of their roles?
❑ Explain the above in a step-wise manner.
For example, how does a cell export a
protein to the extracellular environment?
Lecture 5_Detailed
Organic molecules of
living organisms
CHAPTER TWO
(p. 63 – 76)
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Lecture 5_Detailed
LEARNING OBJECTIVES: LECTURE 5
❑ What are the four biological macromolecules?
❑ Describe and explain the primary structure &
function of each?
❑ Include some examples of each where relevant.
LECTURE 2: HOMEWORK
❑ Animation: monomers and polymers
❑ Animation: lipid structure and function
❑ Animation: protein structure
❑ Animation: nucleic acids
The four major classes of biological
macromolecules
• Carbohydrates
• Lipids
• Proteins
• Nucleic acids
Chemistry background
Carbon the common building block of
organic molecules
• Carbon, the building block of living things
• Comprises 18% of the body by weight
• Forms four covalent bonds
• Can form single or double bonds
• Often bonds with hydrogen, nitrogen, oxygen, or
other carbons
• Can form linear, branched, or ring-shaped
molecules
• Can build micro- or macromolecules
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Figure 2.12 Chemistry background
a) Carbon is the backbone of amino acids, the building
blocks of protein. This amino acid is phenylalanine.
b) In carbon dioxide, c) Lipid molecules (a portion of one
a carbon atom forms is shown here) contain long chains
two covalent bonds of carbon atoms covalently bound
with each oxygen atom. to hydrogen.
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Macromolecules are synthesized and
broken down within the cell
• Dehydration synthesis
• Removes the equivalent of a water molecule to link
molecular units
• Requires energy
• Builds macromolecules from smaller subunits
• Hydrolysis
• Adds the equivalent of a water molecule to break
apart macromolecules
• Releases energy
• Dehydration synthesis is the reverse of hydrolysis
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Figure 2.13 Chemistry background
Simple sugars Carbohydrate
Energy
Energy
Energy
Energy
Energy
Energy
Carbohydrate Simple sugars
a) Dehydration synthesis. b) Hydrolysis.
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Animation: monomers and polymers
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Carbohydrates
• Function: used for energy and structural support
• ‘Structure’: general formula: Cn(H20)n
• Examples: monosaccharides: simple sugars
• glucose
• fructose
• galactose
• ribose
• deoxyribose
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Oligosaccharides: more than one
monosaccharide linked together
• Monosaccharides can be linked together via dehydration
synthesis
• Examples: Disaccharides: two monosaccharides linked
together
• Sucrose: glucose + fructose
• Maltose: glucose + glucose
• Lactose: glucose + galactose
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Figure 2.14
Chemistry background
Ribose Deoxyribose
a) The five-carbon monosaccharides ribose and deoxyribose.
Glucose Fructose
(a monosaccharide) (a monosaccharide)
Sucrose (a disaccharide)
b) Two 6-carbon monosaccharides (glucose and fructose) are
joined together by dehydration synthesis, forming sucrose.
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Polysaccharides store energy
• Polysaccharides
• Thousands of monosaccharides joined in linear
and/or branched chains
• Examples
• Starch: made in plants; stores energy
• Glycogen: made in animals; stores energy
• Cellulose: indigestible polysaccharide made in
plants for structural support
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Figure 2.15
Glucose Glucose Chemistry background
Dehydration
synthesis
a) Dehydration synthesis of
glucose subunits forms
glycogen.
b) A representation of the highly branched nature of glycogen.
Glycogen granules
c) A portion of an animal cell showing granules of stored glycogen
(blue). The large pink structures are mitochondria.
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Lipids
• ‘Structure’/ function: insoluble in water
• Three important classes of lipids
• Examples & function:
• Triglycerides
• Energy storage molecules
• Phospholipids
• Cell membrane structure
• Steroids
• Carbon-based ring structures
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Triglycerides
• are energy-storage molecules
• Also known as fats and oils
• Composed of glycerol and three fatty acids
• Fatty acids
• Saturated (in fats)—all single bonds between
carbons
• Unsaturated (in oils)—include some double bonds
between carbons
• Stored in adipose tissue
• Store energy
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Figure 2.16
Glycerol
Saturated
fatty acid
a) Triglycerides (neutral b) Triglycerides with c) Triglycerides with
fats) are synthesized saturated fatty acids unsaturated fatty
from glycerol and three have straight tails, acids have kinked tails,
fatty acids by allowing them to pack preventing them from
dehydration synthesis. closely together. packing closely together.
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Phospholipids are the primary component of
cell membranes
• Structure
• Glycerol + two fatty acids and phosphate group
• One end of molecule (phosphate and glycerol) is
water soluble (hydrophilic)
• Other end of molecule (2 fatty acid tails) is water
insoluble (hydrophobic)
• Function
• Primary component of cell membranes
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Figure 2.17
Membrane structure
Phosphate
+
Polar head
Glycerol
Fatty acid
Nonpolar tail
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Steroids are composed of four rings
Structure
• Composed of four carbon rings
Examples
• Cholesterol
• Hormones
• Estrogen
• Testosterone
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Figure 2.18
Chemistry background
a) Cholesterol.
A normal
component of
the cell
membrane.
b) Estrogen (estradiol). c) Testosterone.
Female sex hormone Male sex hormone
synthesized from cholesterol. synthesized from cholesterol.
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Animation: lipid structure and function
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Proteins
Structure
• complex, constructed of amino acids
• Long chains (polymers) of subunits called amino acids
• Amino acids
• 20 different types
• Amino end, carboxyl end, R group
• Amino acids are joined by peptide bonds, which are
produced by dehydration synthesis reactions
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Figure 2.19
Amino acids with nonpolar
R groups
Chemistry background
Amino acids with uncharged polar
Alanine (Ala) R groups
Asparagine (Asn)
Isoleucine (Ile)
Cysteine (Cys)
Leucine (Leu) Glutamine (Gln)
Methionine (Met)
Glycine (Gly)
R group =
Phenylalanine (Phe) Serine (Ser) any group in which
carbon or hydrogen
Proline (Pro) Threonine (Thr)
atom is attached to
rest of the molecule
Tryptophan (Trp)
Tyrosine (Tyr)
Amino acids with
Arginine (Arg) positively charged
Valine (Val)
R groups
Amino acids
with Histidine (His)
Aspartic acid (Asp)
negatively
charged
R groups
Glutamic acid (Glu) Lysine (Lys)
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Figure 2.20
Serine (Ser)
Isoleucine (Ile)
Polypeptide
Ser
Ile
Ala
Alanine (Ala)
Val
Valine (Val)
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Structure
• Peptide bond
• Forms between carboxyl end of one amino acid and
amino end of the next amino acid
• Polypeptide
• A polymer of 3–100 amino acids
• Protein
• A polypeptide longer than 100 amino acids that has
a complex structure and function
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• Primary structure
• Amino acid sequence
• Stabilized by peptide bonds
• Secondary structure
• Alpha helix
• Beta pleated sheets
• Stabilized by hydrogen bonds
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• Tertiary structure
• Three-dimensional shape
• Stabilized by disulfide and hydrogen bonds
• Creates polar and nonpolar areas in molecule
• Quaternary structure
• Two or more polypeptide chains are associated
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Figure 2.21 Primary
structure Arg Pro Asp Phe Met Ile Ala
Chemistry background
(sequence of
amino acids)
Hydrogen
bonds
Secondary
structure
(orientation in
space of chains
of amino acids)
Alpha helix Beta sheet
Alpha helix
Tertiary
structure
(three-dimensional
shape)
Random
shape
Beta sheet
Quaternary
structure
(number of polypeptide
chains and their
association)
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Protein function depends on structure
• Denaturation
• Permanent disruption of protein structure
• Can be damaged by temperature or
changes in pH
• Leads to loss of biological function
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Animation: protein structure
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One of several important functions of proteins:
enzymatic activity
• Enzymes
• are proteins
• facilitate biochemical reactions
• function as biological catalysts
• Speed up chemical reactions
• Are not altered or consumed by the reaction
• Without enzymes, many biochemical reactions would
not proceed quickly enough to sustain life
• Maintenance of homeostasis is critical, in order to
maintain the shape and biologic activity of enzymes
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Figure 2.22
Enzyme Reactants
Product
Reactants Enzyme Product is
Approach Reactants
bind to enzyme. changes shape. released.
enzyme.
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One of several important functions of proteins:
enzymatic activity
• The functional shape of an enzyme is dependent on
• temperature
• pH
• ion concentration
• presence of inhibitors
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Nucleic acids
Function: Store genetic information
Structure: Nucleic acids are long chains containing subunits
known as nucleotides
Examples: Two types of nucleic acids
• DNA: deoxyribonucleic acid
• RNA: ribonucleic acid
Function:
• DNA contains the instructions for producing RNA
• RNA contains the instructions for producing proteins
• Proteins direct most life processes
• DNA → RNA → Proteins
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Nucleic acids (continued)
Structure:
• Nucleotides
• Building blocks (monomers) of nucleic acids
• Each nucleotide contains
• 5 carbon sugar
• Deoxyribose (in DNA nucleotides)
• Ribose (in RNA nucleotides)
• Nitrogenous base
• Phosphate group
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Figure 2.23
Adenine (A) Thymine (T) Cytosine (C)
Guanine (G)
Phosphate
Deoxyribose
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Nucleic acids (continued)
• Structure of DNA (deoxyribonucleic acid)
• Double-stranded
• Nucleotides contain
• Deoxyribose (sugar)
• Nitrogenous bases
• Adenine
• Guanine
• Cytosine
• Thymine
• Pairing
• Adenine – Thymine
• Guanine – Cytosine
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Figure 2.24
C G
A T
Hydrogen bonds
G
G C Base pair
Double-stranded T
A
Phosphate
T Sugar
A P
Nucleotide
P
C G
P
P
A
G C
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Nucleic acids (continued)
• Structure of RNA (ribonucleic acid)
• Single-stranded
• Nucleotides contain
• Ribose
• Nitrogenous bases
• Adenine
• Guanine
• Cytosine
• Uracil
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Figure 2.25
Phosphate
P Ribose
Single-stranded C
P
A
P
Uracil (U)
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Animation: nucleic acids
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RECAP THIS LECTURE (L 5)
❑ What are the four biological macromolecules?
❑ Describe and explain the primary structure &
function of each?
❑ Include some examples of each where relevant.
LECTURE 5: HOMEWORK
❑ Animation: monomers and polymers
❑ Animation: lipid structure and function
❑ Animation: protein structure
❑ Animation: nucleic acids
Next: the cell cycle & the Central Dogma
CHAPTER 17
(p. 431 – 438)
© 2017 Pearson Education, Ltd.
