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Organic molecules of
living organisms
CHAPTER TWO
(p. 63 – 76)
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
• 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
© 2017 Pearson Education, Ltd.
Figure 2.13 Chemistry background
Simple sugars Carbohydrate
Energy
Energy
Energy
Energy
Energy
Energy
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.
© 2017 Pearson Education, Ltd.
Polysaccharides store energy
• Polysaccharides
• Examples
Dehydration
synthesis
a) Dehydration synthesis of
glucose subunits forms
glycogen.
Glycogen granules
• Fatty acids
• Store energy
© 2017 Pearson Education, Ltd.
Figure 2.16
Glycerol
Saturated
fatty acid
• Structure
• Function
Membrane structure
Phosphate
+
Polar head
Glycerol
Fatty acid
Nonpolar tail
Structure
Examples
• Cholesterol
• Hormones
• Estrogen
• Testosterone
a) Cholesterol.
A normal
component of
the cell
membrane.
• Amino acids
• 20 different types
Isoleucine (Ile)
Cysteine (Cys)
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 Histidine (His)
Aspartic acid (Asp)
negatively
charged
R groups
Serine (Ser)
Isoleucine (Ile)
Polypeptide
Ser
Ile
Ala
Alanine (Ala)
Val
Valine (Val)
© 2017 Pearson Education, Ltd.
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
• Secondary structure
• Alpha helix
• Beta pleated sheets
• Stabilized by hydrogen bonds
• Quaternary structure
• Two or more polypeptide chains are associated
Hydrogen
bonds
Secondary
structure
(orientation in
space of chains
of amino acids)
Alpha helix
Tertiary
structure
(three-dimensional
shape)
Random
shape
Beta sheet
Quaternary
structure
(number of polypeptide
chains and their
association)
• Denaturation
• Permanent disruption of protein structure
• Can be damaged by temperature or
changes in pH
Enzyme Reactants
Product
• temperature
• pH
• ion concentration
• presence of inhibitors
Structure:
• Nucleotides
• Building blocks (monomers) of nucleic acids
Deoxyribose
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
• Guanine
• Cytosine
• Uracil
© 2017 Pearson Education, Ltd.
Figure 2.25
Phosphate
P Ribose
Single-stranded C
P
A
P
Uracil (U)
function of each?
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)