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The Structure and Function of Large Biological Molecules

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Title: The Structure and Function of Large Biological Molecules


1
The Structure and Function of Large Biological
Molecules
  • Chapter 5

2
Polymers
  • What is a polymer?
  • Poly many mer part. A polymer is a large
    molecule consisting of many smaller sub-units
    bonded together
  • What is a monomer?
  • A monomer is a sub-unit of a polymer

3
Making and Breaking Polymers
  • How are covalent linkages between monomers formed
    in the creation of organic polymers?
  • Condensation or dehydration synthesis reactions.
  • Monomers are covalently linked to one another
    through the removal of water.

4
Dehydration reaction
5
Hydrolysis
  • What is a hydrolysis reaction?
  • Polymers are broken down into monomers
  • Hydro water lysis loosening
  • Water is added and the lysis of the polymer occurs

6
Hydrolysis
7
Classes of Organic Molecules
  • What are the four classes of organic molecules?
  • Carbohydrates
  • Lipids
  • Proteins
  • Nucleic Acids

8
Carbohydrates
  • Sugars
  • Carbo carbon, hydrate water carbohydrates
    have the molecular formula (CH2O)n
  • Functions
  • Store energy in chemical bonds
  • Glucose is the most common monosaccharide
  • Glucose is produced by photosynthetic autotrophs

9
Structure of Monosaccharides
  • An OH group is attached to each carbon except
    one, which is double bonded to an oxygen
    (carbonyl).

10
Monosaccharides
  • Classified according to the size of their carbon
    chains, varies from 3 to 7 carbons.

Triose 3 carbons
Pentose 5 carbons
Hexose 6 carbons
11
In aqueous solutions, many monosaccharides form
rings
12
Structure of Disaccharides
  • Double sugar that consists of 2 monosaccharides,
    joined by a glycosidic linkage
  • What reaction forms the glycosidic linkage?
  • Dehydration reaction

13
Examples of Disaccharides
  • Lactose glucose galactose

Sucrose glucose fructose
14
Polysaccharides
  • Structure Polymers of a few hundred or a few
    thousand monosaccharides
  • Functions energy storage molecules or for
    structural support

15
Polysaccharides
  • Starch is a plant storage form of energy, easily
    hydrolyzed to glucose units
  • Cellulose is a fiber-like structural material -
    tough and insoluble - used in plant cell walls
  • Glycogen is a highly branched chain used by
    animals to store energy in muscles and the liver
  • Chitin is a polysaccharide used as a structural
    material in arthropod exoskeleton and fungal cell
    walls

16
Lipids
  • Structure Greasy or oily nonpolar compounds
  • Functions
  • Energy storage
  • membrane structure
  • Protecting against desiccation (drying out)
  • Insulating against cold
  • Absorbing shocks
  • Regulating cell activities by hormone actions

17
Structure of Fatty Acids
  • Long chains of mostly carbon and hydrogen atoms
    with a -COOH group at one end
  • When they are part of lipids, the fatty acids
    resemble long flexible tails

18
Saturated and Unsaturated Fats
  • Unsaturated fats
  • liquid at room temp
  • one or more double bonds between carbons in the
    fatty acids allows for kinks in the tails
  • most plant fats
  • Saturated fats
  • have only single C-C bonds in fatty acid tails
  • solid at room temp
  • most animal fats

19
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20
Saturated fatty acid
21
Saturated fatty acid
Unsaturated fatty acid
22
Structure of Triglycerides
  • Glycerol 3 fatty acids
  • 3 ester linkages are formed between a hydroxyl
    group of the glycerol and a carboxyl group of the
    fatty acid

23
Phospholipids
  • Structure Glycerol 2 fatty acids phosphate
    group
  • Function Main structural component of
    membranes, where they arrange in bilayers

24
Phospholipids in Water
25
Waxes
  • Function
  • Lipids that serve as coatings for plant parts and
    as animal coverings.

26
Steroids
  • Structure Four carbon rings with no fatty acid
    tails
  • Functions
  • Component of animal cell membranes
  • Modified to form sex hormones

27
Proteins
  • Structure
  • Polypeptide chains
  • Consist of peptide bonds between 20 possible
    amino acid monomers
  • Have a 3 dimensional globular shape

28
Functions of Proteins
  • Enzymes which accelerate specific chemical
    reactions up to 10 billion times faster than they
    would spontaneously occur
  • Structural materials, including keratin (the
    protein found in hair and nails) and collagen
    (the protein found in connective tissue)

29
Functions of Proteins
  • Specific binding, such as antibodies that bind
    specifically to foreign substances to identify
    them to the body's immune system
  • Specific carriers, including membrane transport
    proteins that move substances across cell
    membranes, and blood proteins, such as
    hemoglobin, that carry oxygen, iron, and other
    substances through the body

30
Functions of Proteins
  • Contraction, such as actin and myosin fibers that
    interact in muscle tissue
  • Signaling, including hormones such as insulin
    that regulate sugar levels in blood

31
Structure of Amino Acid Monomers
  • Consist of an asymmetric carbon covalently
    bonded to
  • Hydrogen
  • Amino group
  • Carboxyl (acid) group
  • Variable R group specific to each amino acid

32
Properties of Amino Acids
  • Grouped by polarity
  • Variable R groups (side chains) confer different
    properties to each amino acid
  • polar, water soluble
  • non-polar, water insoluble
  • positively charged
  • negatively charged

33
Levels of Protein Structure
  • Primary
  • Secondary
  • Tertiary
  • Quaternary

34
Primary Structure
  • Unique sequence of amino acids in a protein
  • Slight change in primary structure can alter
    function
  • Determined by genes
  • Condensation synthesis reactions form the peptide
    bonds between amino acids

35
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36
Secondary Structure
  • Repeated folding of proteins polypeptide
    backbone
  • stabilized by H bonds between peptide linkages in
    the proteins backbone
  • 2 types, alpha helix, beta pleated sheets

37
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38
Tertiary Structure
  • Irregular contortions of a protein due to bonding
    between R groups
  • Weak bonds
  • H bonding between polar side chains
  • ionic bonding between charged side chains
  • hydrophobic and van der Waals interactions
  • Strong bonds
  • disulfide bridges form strong covalent linkages

39
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40
Quaternary Structure
  • Results from interactions among 2 or more
    polypeptides

41
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42
Factors That Determine Protein Conformation
  • Occurs during protein synthesis within cell
  • Depends on physical conditions of environment
  • pH, temperature, salinity, etc
  • Change in environment may lead to denaturation of
    protein
  • Denatured protein is biologically inactive
  • Can renature if primary structure is not lost

43
Nucleic Acids
  • Two kinds
  • DNA
  • double stranded
  • can self replicate
  • makes up genes which code for proteins
  • is passed from one generation to another
  • RNA
  • single stranded
  • functions in actual synthesis of proteins coded
    for by DNA
  • is made from the DNA template molecule

44
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45
Nucleotide Monomer Structure
  • Both DNA and RNA are composed of nucleotide
    monomers
  • Nucleotide 5 carbon sugar, phosphate, and
    nitrogenous base

Deoxyribose in DNA
Ribose in RNA
46
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47
Building the Polymer
  • Phosphate group of one nucleotide forms strong
    covalent bond with the 3 carbon of the sugar of
    the other nucleotide.

48
Functions of Nucleotides
  • Monomers for Nucleic Acids
  • Transfer chemical energy from one molecule to
    another (e.g. ATP)

49
  • DNA
  • Double helix
  • 2 polynucleotide chains wound into the double
    helix
  • Base pairing between chains with H bonds
  • A - T
  • C - G

50
Summary of the Organic Molecules
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