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Ch. 5 Structure and
Function of
Macromolecules
AP Biology
Macromolecules
• Most are polymers
• Polymer
– Large molecule consisting
of many identical or similar
building blocks linked by
bonds
• Monomer
– Subunits that serve as
building blocks for
polymers
Polyethene is a thermoplastic commodity heavily
used in consumer products (over 60 million tons are
produced worldwide every year).
A limitless variety of polymers can be
built from a small set of monomers
• Inherent differences between
siblings result from variations
in polymers
• Construction of
macromolecules
– 40-50 common monomers and
others that occur rarely
– Small molecules that are
common to all organisms are
ordered into unique
macromolecules
How Cells Use Organic
Compounds
• Biological organisms use the
same kinds of building blocks.
• All macromolecules (large,
complex molecules) have
specific functions in cells.
• Other than water,
macromolecules make up the
largest percent mass of a cell.
Condensation and Hydrolysis
• Condensation reactions
– Dehydration reactions
– When two molecules
become covalently
bonded to each other
through the loss of a small
molecule, usually water
• Hydrolysis
– Separation of two
molecules by the addition
of a water molecule
• Large polymers form from smaller
monomers.
• New properties emerge.
• Living cells require/synthesize:
– Carbohydrates
– Lipids
– Proteins
– Nucleic Acids
The Molecules of Life
• Used as fuel and building material
• Carbs are sugars and their polymers
• Main types:
– Monosaccharides
– Disaccharides
– Polysaccharides
Carbohydrates
Monosaccharides (CH2O)
• Generally have
molecular formulas in
some multiple of CH2O
• Glucose (C6H12O6) is
most common
• In aqueous solution
may form rings
• Major nutrients for cells
Disaccharides
• Two monosaccharides joined by glycosidic
linkages
• Glycosidic linkage
– A covalent bond formed between monosaccharides
• Sucrose is most prevalent
Dissacharide
Formation
Polysaccharides
• 100s to 1000s of
monosaccharides long
• Starch
– Storage poly. of plants
• Glycogen
– Storage poly. of animals
• Cellulose
– Structural poly. which is a major
component of tough plant cell walls
• Chitin
– Structural poly. used by arthropods
to build exoskeletons
Starch &
Cellulose
Forms ring in
aqueous
solution
Lipids
• Mostly hydrophobic
molecules with diverse
functions
• Little or no affinity for water
• Used for energy storage
and structure
• Main types:
– Fats
– Phospholipids
– Steroids
Fats
• Large molecules, but not
polymers
• Fatty acid
– A long carbon skeleton
with carboxyl group head
and a hydrocarbon tail
14
Triacylglycerol (Triglyceride)
• Three fatty acids
linked to one
glycerol molecule
Saturated & Unsaturated
Fats
• Saturated fatty acids
– Fatty acid containing no
double bonds between
the carbon atoms
composing the tail
– Solids at room temp.
• Unsaturated fatty acids
– Has one or more double
bonded carbons in the
tail
Phospholipids
• Two fatty acid tails linked to one glycerol
molecule
– Ambivalent behavior toward water
– When in contact with water they form a micelle
(cluster)
Steroids
• Lipids characterized by
a carbon skeleton,
consisting of 4
interconnected rings
• Cholesterol
– Important steroid that is a
common component of
the membranes of animal
cells
– Many hormones are
steroids produced from
cholesterol
Proteins
• The molecular tools for most cellular
functions
• Used for:
– Structural support
– Storage
– Transport of other substances
– Signaling from one part of the organism to the
other
– Movement
– Defense against foreign substances
• Conformation
– Unique 3-D shape of a protein
Protein Polypeptides
• Polymers of amino
acids connected in a
specific sequence
• Amino acids
– Organic molecules
possessing both
carboxyl and amino
groups
• Acidity is determined
by side chains
Peptide Bonds
• Formed when an
enzyme joins amino
acids by means of
condensation
• Polypeptide
– Chains of amino acids
linked by peptide
bonds
• Conformation (shape) determines function
and is the result of the linear sequence of
amino acids in a polypeptide.
• Folding, coiling and the interactions of
multiple polypeptide chains create a
functional protein
• 4 levels of conformation
– Primary
– Secondary
– Tertiary
– Quartinary
Protein Conformation
Primary Structure
• Unique, linear
sequence of amino
acids in a protein
• A change in one a.a.
can effect every other
level of structure
– ex. point mutation in
hemoglobin
Secondary Structure
• Hydrogen bonding
occurs between amino
and carbonyl groups
of amino acids.
• Structures Formed:
• α Helix: Common in fibrous
proteins, creates “elastic”
properties.
• β Sheet: Anti-parallel
chains form sheet.
Tertiary Structure
• Irregular contortions from bonding
between side chains of various amino
acids
25
Quartinary Structure
• Overall protein structure that results
from aggregation of tertiary subunits
Denaturation
• Unraveling and loss of native
conformation of a protein
• Can be due to heat, pH, salts, etc.
• Some can renature exactly, others
cannot
• Ex: cooking an egg
Nucleic Acids
• Store and transmit hereditary information
• Gene
– A unit of inheritance
• DNA & RNA
– Deoxyribonucleic acid & Ribonucleic acid
– DNA is like computer software, proteins are like
hardware
– Genetic info flows from DNA  RNA  protein
DNA Structure
• A polymer with an
information-rich sequence
of nucleotides
• Pyrimidine
– 6 membered ring made of
carbon and nitrogen atoms
– Cytosine and thymine
• Purine
– 6 membered ring fused to a
five membered ring
– Adenine and guanine
• Phosphodiester
– Covelent bonds holding
nucleotides together
DNA Structure, cont.
• Double helix
– Two chains of nucleotides
that spiral around an
imaginary axis
• Hydrogen bonds
– Hold two chains of
nucleotides together
• Adenine pairs with
thymine
• Cytosine pairs with
guanine
• Two strands of DNA
double helix are
complimentary
RNA
• Single stranded
• Four kinds of
nucleotide monomers
(A, U, C, G)
• Key players in the
protein-building
processes
• mRNA, tRNA, rRNA
DNA & Protein Importance
• Inheritance is based on precise
replication of DNA
• We can use DNA and proteins as “tape
measures” of evolution
– Linear sequences of nucleotides in DNA
molecules are passed from parents to
offspring
– More distantly related species have chains
that are less similar
Review questions
• Section 4.1 page 59, number 1
• Read Inquiry 4.2. Think about the what if question.
• Section 5.1 page 69, number 1
• Section 5.2 page 74, number 3
• Self quiz page 91 numbers 1-8.
AP BIO MACROMOLECULES Chapter 5 review.ppt

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AP BIO MACROMOLECULES Chapter 5 review.ppt

  • 1. Ch. 5 Structure and Function of Macromolecules AP Biology
  • 2. Macromolecules • Most are polymers • Polymer – Large molecule consisting of many identical or similar building blocks linked by bonds • Monomer – Subunits that serve as building blocks for polymers Polyethene is a thermoplastic commodity heavily used in consumer products (over 60 million tons are produced worldwide every year).
  • 3. A limitless variety of polymers can be built from a small set of monomers • Inherent differences between siblings result from variations in polymers • Construction of macromolecules – 40-50 common monomers and others that occur rarely – Small molecules that are common to all organisms are ordered into unique macromolecules
  • 4. How Cells Use Organic Compounds • Biological organisms use the same kinds of building blocks. • All macromolecules (large, complex molecules) have specific functions in cells. • Other than water, macromolecules make up the largest percent mass of a cell.
  • 5. Condensation and Hydrolysis • Condensation reactions – Dehydration reactions – When two molecules become covalently bonded to each other through the loss of a small molecule, usually water • Hydrolysis – Separation of two molecules by the addition of a water molecule
  • 6. • Large polymers form from smaller monomers. • New properties emerge. • Living cells require/synthesize: – Carbohydrates – Lipids – Proteins – Nucleic Acids The Molecules of Life
  • 7. • Used as fuel and building material • Carbs are sugars and their polymers • Main types: – Monosaccharides – Disaccharides – Polysaccharides Carbohydrates
  • 8. Monosaccharides (CH2O) • Generally have molecular formulas in some multiple of CH2O • Glucose (C6H12O6) is most common • In aqueous solution may form rings • Major nutrients for cells
  • 9. Disaccharides • Two monosaccharides joined by glycosidic linkages • Glycosidic linkage – A covalent bond formed between monosaccharides • Sucrose is most prevalent
  • 11. Polysaccharides • 100s to 1000s of monosaccharides long • Starch – Storage poly. of plants • Glycogen – Storage poly. of animals • Cellulose – Structural poly. which is a major component of tough plant cell walls • Chitin – Structural poly. used by arthropods to build exoskeletons
  • 12. Starch & Cellulose Forms ring in aqueous solution
  • 13. Lipids • Mostly hydrophobic molecules with diverse functions • Little or no affinity for water • Used for energy storage and structure • Main types: – Fats – Phospholipids – Steroids
  • 14. Fats • Large molecules, but not polymers • Fatty acid – A long carbon skeleton with carboxyl group head and a hydrocarbon tail 14
  • 15. Triacylglycerol (Triglyceride) • Three fatty acids linked to one glycerol molecule
  • 16. Saturated & Unsaturated Fats • Saturated fatty acids – Fatty acid containing no double bonds between the carbon atoms composing the tail – Solids at room temp. • Unsaturated fatty acids – Has one or more double bonded carbons in the tail
  • 17. Phospholipids • Two fatty acid tails linked to one glycerol molecule – Ambivalent behavior toward water – When in contact with water they form a micelle (cluster)
  • 18. Steroids • Lipids characterized by a carbon skeleton, consisting of 4 interconnected rings • Cholesterol – Important steroid that is a common component of the membranes of animal cells – Many hormones are steroids produced from cholesterol
  • 19. Proteins • The molecular tools for most cellular functions • Used for: – Structural support – Storage – Transport of other substances – Signaling from one part of the organism to the other – Movement – Defense against foreign substances • Conformation – Unique 3-D shape of a protein
  • 20. Protein Polypeptides • Polymers of amino acids connected in a specific sequence • Amino acids – Organic molecules possessing both carboxyl and amino groups • Acidity is determined by side chains
  • 21. Peptide Bonds • Formed when an enzyme joins amino acids by means of condensation • Polypeptide – Chains of amino acids linked by peptide bonds
  • 22. • Conformation (shape) determines function and is the result of the linear sequence of amino acids in a polypeptide. • Folding, coiling and the interactions of multiple polypeptide chains create a functional protein • 4 levels of conformation – Primary – Secondary – Tertiary – Quartinary Protein Conformation
  • 23. Primary Structure • Unique, linear sequence of amino acids in a protein • A change in one a.a. can effect every other level of structure – ex. point mutation in hemoglobin
  • 24. Secondary Structure • Hydrogen bonding occurs between amino and carbonyl groups of amino acids. • Structures Formed: • α Helix: Common in fibrous proteins, creates “elastic” properties. • β Sheet: Anti-parallel chains form sheet.
  • 25. Tertiary Structure • Irregular contortions from bonding between side chains of various amino acids 25
  • 26. Quartinary Structure • Overall protein structure that results from aggregation of tertiary subunits
  • 27.
  • 28. Denaturation • Unraveling and loss of native conformation of a protein • Can be due to heat, pH, salts, etc. • Some can renature exactly, others cannot • Ex: cooking an egg
  • 29. Nucleic Acids • Store and transmit hereditary information • Gene – A unit of inheritance • DNA & RNA – Deoxyribonucleic acid & Ribonucleic acid – DNA is like computer software, proteins are like hardware – Genetic info flows from DNA  RNA  protein
  • 30. DNA Structure • A polymer with an information-rich sequence of nucleotides • Pyrimidine – 6 membered ring made of carbon and nitrogen atoms – Cytosine and thymine • Purine – 6 membered ring fused to a five membered ring – Adenine and guanine • Phosphodiester – Covelent bonds holding nucleotides together
  • 31. DNA Structure, cont. • Double helix – Two chains of nucleotides that spiral around an imaginary axis • Hydrogen bonds – Hold two chains of nucleotides together • Adenine pairs with thymine • Cytosine pairs with guanine • Two strands of DNA double helix are complimentary
  • 32. RNA • Single stranded • Four kinds of nucleotide monomers (A, U, C, G) • Key players in the protein-building processes • mRNA, tRNA, rRNA
  • 33. DNA & Protein Importance • Inheritance is based on precise replication of DNA • We can use DNA and proteins as “tape measures” of evolution – Linear sequences of nucleotides in DNA molecules are passed from parents to offspring – More distantly related species have chains that are less similar
  • 34. Review questions • Section 4.1 page 59, number 1 • Read Inquiry 4.2. Think about the what if question. • Section 5.1 page 69, number 1 • Section 5.2 page 74, number 3 • Self quiz page 91 numbers 1-8.