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Title: BASIC CHEMISTRY


1
BASIC CHEMISTRY
2
WHAT WILL WE COVER?
  • Matter, elements, and atoms
  • Atomic structure
  • Chemical bonds
  • Chemistry of water
  • Acids, bases, and pH
  • Macromolecule structure and function

3
MATTER
  • Matter is defined as anything possessing mass and
    taking up space
  • Tangible
  • Can exist in various forms
  • Solid
  • Liquid
  • Gas
  • Comprised of many elements

4
ELEMENTS
  • An element cannot be broken down into simpler
    substances by normal chemical means
  • Approximately 100 different elements exist
  • Each is denoted by a symbol
  • e.g., Carbon (C), hydrogen (H), etc.
  • e.g., NOT water (H2O), glucose, etc.

X
Chlorine (Cl)
Sodium Chloride (NaCl)
Sodium (Na)
5
ELEMENTS
  • About 25 elements are known to be essential to
    life
  • 96 of the mass of living things is comprised
    of just four elements
  • Carbon (C)
  • Hydrogen (H)
  • Nitrogen (N)
  • Oxygen (O)

6
ATOMS
  • An atom is the smallest unit into which an
    element can be subdivided while retaining its
    properties
  • Comprised of smaller subatomic particles
  • Protons charge mass 1 amu
  • Neutrons no charge mass 1 amu
  • Electrons - charge mass ltltlt 1 amu
  • (1 atomic mass unit (amu) 1 Dalton 1.7
    10-24 g)

7
ATOMIC STRUCTURE
  • Protons and neutrons form an atoms nucleus
  • Electrons are present outside of the nucleus

Helium (He) atom
8
ATOMIC NUMBER
  • Atoms of different elements possess different
    numbers of protons
  • The number of protons in an atom is termed its
    atomic number
  • This number defines the element

1
2
3
9
ATOMIC MASS
  • Protons and neutrons have significant mass
  • The number of protons plus neutrons in an atom is
    termed its atomic mass
  • Electrons have negligible mass
  • This number is slightly variable for many elements

1
4
7
H
Li
He
1
2
3
10
ISOTOPES
  • Isotopes are atoms of the same element possessing
    different atomic masses
  • Due to different numbers of neutrons
  • Identical chemical behavior

1
2
3
H
H
H
1
1
1
11
ISOTOPES
  • Some isotopes are stable
  • e.g., 1H, 2H, 12C, 13C, etc.
  • Some isotopes are unstable
  • e.g., 3H, 14C, 32P, 35S, etc.
  • Radioactive

12
ISOTOPES
  • Radioactive isotopes
  • Decay at a constant rate into more stable forms
  • May decay into another element
  • e.g., 14C ? N
  • Various uses
  • Important research tools
  • Monitor biological processes
  • Diagnostic tools in medicine
  • Determine age of fossils
  • Sometimes produce superheroes

13
ISOTOPES
  • Each radioactive isotope has a fixed rate of
    decay
  • Unaffected by temperature, pressure etc.
  • The time required for half of a sample to decay
    is termed the radioisotopes half-life
  • e.g., Half-life of 14C is 5,730 years

14
ISOTOPES
  • Fossils contain isotopes of elements that
    accumulated while they were alive
  • Accumulation stops upon death
  • Death tends to reduce ones appetite
  • Accumulated isotopes slowly decay into more
    stable isotopes

15
ISOTOPES
  • Ages of fossils can be determined using
    radiometric dating
  • Compares accumulating daughter isotope to
    remaining parent isotope
  • e.g., Carbon dating is useful for dating fossils
    up to 75,000 years old
  • 13 half-lives
  • Radioisotopes with longer half-lives can be
    used to date older fossils

16
ELECTRON SHELLS
  • Electrons vary in the amount of energy they
    possess
  • Each electron exists within a discrete energy
    level
  • These energy levels are represented by electron
    shells
  • Most atoms possess multiple electron shells

17
ELECTRON SHELLS
  • Electrons exist within electron shells
  • The first shell must be completely filled before
    electrons are placed in the second shell, etc.
  • The first shell can hold 2 electrons
  • The next few electrons can each hold 8 electrons

18
CHEMICAL BONDS
  • Atoms are most stable when their outermost
    electron shell is completely full
  • Making and breaking chemical bonds involves the
    exchange or rearrangement of electrons
  • Atoms will tend to react such that their
    outermost electron shell becomes completely full

19
CHEMICAL BONDS
  • How would you expect F and Cl to react?
  • Li and Na?
  • He, Ne, and Ar?

20
IONS
  • A sodium atom possesses a single electron in its
    outermost electron shell
  • Tends to lose this electron
  • Loss of the electron produces a sodium ion
  • A charged form of a sodium atom

21
IONS
  • A chlorine atom possesses seven electrons in its
    outermost electron shell
  • Tends to gain a single electron
  • Gain of this electron produces a chloride ion
  • A charged form of a chlorine atom

22
IONIC BONDS
  • The attraction between oppositely charged ions is
    termed an ionic bond
  • Compounds formed by ionic bonds are called ionic
    compounds or salts
  • Indefinite size and number of ions
  • Ions present in a fixed ratio
  • e.g., 11 ratio in NaCl

23
COVALENT BONDS
  • Electrons are not always gained or lost
  • Molecules can be formed when electrons are shared
  • Sharing is always in pair(s) of electrons
  • Shared electrons contribute to electron shells of
    both atoms
  • This sharing of electrons is termed a covalent
    bond

24
COVALENT BONDS
  • The sharing of a pair of electrons forms a
    covalent bond
  • A double covalent bond involves the sharing of
    two pairs of electrons
  • A triple covalent bond involves the sharing of
    three pairs of electrons

25
COVALENT BONDS
  • Electron sharing can be equal or unequal
  • Equal sharing results in no separation of charges
  • Nonpolar covalent bonds

Methane
26
COVALENT BONDS
  • Electron sharing can be equal or unequal
  • Unequal sharing results in a separation of
    charges
  • Polar covalent bonds
  • Electronegative atoms such as oxygen and nitrogen
    tend to attract electrons more strongly than
    carbon or hydrogen
  • They thereby possess partial negative charges

27
COVALENT BONDS
  • Water is a polar molecule
  • The hydrogen atoms possess partial positive
    charges
  • The oxygen atom possesses a partial negative
    charge

28
HYDROGEN BONDS
  • Attraction between a hydrogen atom bearing a
    partial positive charge and another atom bearing
    a partial negative charge
  • Much weaker than covalent or ionic bonds
  • 1/20 as strong
  • Many weak bonds can add up to a significant
    force
  • Transient
  • Constantly breaking and reforming

29
CHEMISTRY OF WATER
  • Water is a critically important molecule
  • Most of the Earths surface is submerged in water
  • Life on Earth began in water
  • Life evolved in water for 3 billion years
    before spreading onto land
  • The abundance of water is a major reason why
    the Earth is habitable

30
CHEMISTRY OF WATER
  • Water is the most prevalent molecule within
    living organisms
  • Cells are about 70 95 water
  • Most cells are themselves surrounded by water

31
CHEMISTRY OF WATER
  • Water molecules possess polar covalent bonds
  • Able to participate in H-bonds
  • Water molecules interact with each other
  • Water is held together by these H-bonds
  • Cohesion
  • Water attaches to other ions and molecules
  • Adhesion

32
CHEMISTRY OF WATER
  • Cohesion and adhesion allow transport of water
    against gravity
  • Fluid movement into capillary tubes or xylem
    vessels
  • Capillary action

33
CHEMISTRY OF WATER
  • Surface tension results from cohesion
  • Difficult to break the surface of water
  • e.g., Water strider, skipping rocks, etc.

34
WATER AS A SOLVENT
  • Water is a powerful and versatile solvent
  • A wide variety of molecules and ions dissolve in
    water
  • e.g., Sugars, salts, some proteins, etc.
  • Interacts well with polar or charged molecules
    and ions
  • Most chemical reactions within organisms occur in
    a water medium

35
WATER AS A SOLVENT
  • Polar or charged molecules and ions are
    hydrophilic
  • Interact favorably with water
  • Hydration shells surround ions from salts
  • Similar structures surround polar molecules

36
WATER AS A SOLVENT
  • Many molecules and ions dissolve in water
  • A solution is formed
  • Water is the solvent
  • The salt, sugar, dye, etc. is the solute
  • A solution in which water is the solvent is
    termed an aqueous solution

Chicago River before St. Patrick's Day
37
WATER AS A SOLVENT
  • Not all hydrophilic molecules dissolve in water
  • Typical of very large hydrophilic molecules
  • e.g., Cotton consists of very large molecules of
    cellulose
  • A towel dries your body, but does not dissolve in
    the water

38
DISSOCIATION OF WATER
  • Most water molecules exist as H2O (H-O-H)
  • A small fraction of water molecules exist in a
    dissociated state
  • 1 in 554 million molecules in pure water
  • A hydrogen atom shifts from one water molecule to
    another
  • H-O-H ? H OH- (hydrogen ion hydroxide ion)
  • 2H2O ? H3O OH- (hydronium ion hydroxide ion)

39
DISSOCIATION OF WATER
  • H and OH- are formed when H2O dissociates
  • Very reactive
  • Equal concentrations in pure water
  • 10-7 mol/L
  • Concentrations are not always equal
  • Can be altered by the addition of acids or bases
  • As H ?, OH- ?, and vice versa

40
ACIDS, BASES, AND pH
  • An acid is a substance that increases the H
    concentration of a solution
  • Generally donates additional H
  • e.g., HCl ? H Cl-
  • A base is a substance that decreases the H
    concentration of a solution
  • Either absorbs H or donates OH-
  • e.g., NH3 H ? NH4
  • e.g., NaOH ? Na OH-

41
ACIDS, BASES, AND pH
  • pH is a quantitative measure of H
  • Pure water is pH 7 (neutral)
  • Equal concentrations of H and OH-
  • Acidic solution contain more H than OH-
  • pH lt 7
  • Basic solutions contain more OH- than H
  • pH gt 7

42
ACIDS, BASES, AND pH
  • pH is a quantitative measure of H
  • Ranges from 0 (most acidic) to 14 (most basic)
  • Each pH unit represents a tenfold change in the
    concentration of H
  • e.g., pH 4 has 100 times more H than pH 6

43
ACIDS, BASES, AND pH
  • The interior pH of most cells is close to 7
  • Even slight changes in pH can be harmful to cells
    and organisms
  • Chemical processes of the cell are very sensitive
    to concentrations of H and OH-
  • The shapes of biological molecules can be altered
    by changes in H and OH- concentrations
  • e.g., Enzymes, etc.
  • Altered shape can reduce function
  • Biological fluids contain buffers
  • Substances or systems that minimize changes in pH
    by accepting or donating H

44
ACID PRECIPITATION
  • Acid precipitation represents a serious assault
    on water quality
  • Uncontaminated rain has a pH of about 5.6
  • Slightly acidic due to carbonic acid formed from
    dissolved CO2
  • CO2 H2O ? H2CO3 ? H HCO3-
  • Acid precipitation is more acidic than this
  • pH 4.3 rain has been measured in the U.S.
  • 20 times more acidic than normal rain

45
ACID PRECIPITATION
  • Acid precipitation
  • Caused primarily by the presence in the
    atmosphere of sulfur oxides and nitrogen oxides
  • React with water to form strong acids
  • Fall to earth with rain or snow

46
ACID PRECIPITATION
  • Acid precipitation
  • The burning of fossil fuels in factories and
    automobiles is a major source of acid
    precipitation
  • Electrical power plants burning coal produce more
    of these pollutants than any other source
  • Winds carry these pollutants away
  • Acid rain may fall far from industrial centers

47
ACID PRECIPITATION
  • Acid precipitation
  • Can damage life in lakes and streams
  • Can remove mineral ions from soil
  • e.g., Calcium and magnesium ions
  • Essential nutrients
  • Ordinarily help to buffer soil
  • Can increase the solubility of certain ions
  • e.g., Aluminum can reach toxic concentrations

48
BIOLOGICAL MACROMOLECULES
49
CELL COMPOSITION
  • Cell composition
  • 70 95 water
  • Most of the remainder of the cell is composed of
    organic molecules
  • Molecules containing both carbon (C) and
    hydrogen (H)

50
MACROMOLECULES
  • There are four major classes of large biological
    molecules
  • Carbohydrates
  • Lipids
  • Nucleic acids
  • Proteins

51
MACROMOLECULES
  • Three of the four classes of macromolecules are
    polymers
  • Long molecules assembled from many similar or
    identical monomers

52
MACROMOLECULES
  • Monomers are covalently linked via condensation
    reactions
  • a.k.a. Dehydration reactions
  • Two monomers are covalently linked to each other
    through the loss of a water molecule
  • -H is removed from one monomer
  • -OH is removed from the other monomer
  • H2O is formed

53
MACROMOLECULES
  • Polymers can be disassembled into monomers via
    hydrolysis reactions
  • Essentially a condensation reaction in reverse
  • Covalent bond between monomers is broken through
    the addition of water
  • -H is added to one monomer
  • -OH is added to the other monomer

54
MACROMOLECULES
55
CARBOHYDRATES
  • Sugars and their polymers
  • General formula (CH2O)n
  • CHO ratio 121
  • Possess numerous polar covalent bonds
  • Form H-bonds
  • Interact favorably with water
  • Hydrophilic

56
ROLES OF CARBOHYDRATES
  • Key roles of carbohydrates
  • Short-term energy storage
  • Longer-term energy storage
  • Structural roles
  • Cell communication

57
ROLES OF CARBOHYDRATES
  • Short-term energy storage
  • Monosaccharides (simple sugars) are the
    simplest carbohydrates
  • e.g., Glucose, fructose, galactose, ribose, etc.
  • Readily burned to release energy

58
ROLES OF CARBOHYDRATES
  • Short-term energy storage
  • Disaccharides consists of two covalently linked
    monosaccharides
  • e.g., Sucrose, lactose, maltose, etc.
  • Readily hydrolyzed to form monosaccharides

59
LACTOSE INTOLERANCE
  • Virtually all humans can digest lactose during
    infancy and early childhood
  • Milk is an important food source early in life
  • Infants produce the enzyme lactase
  • Hydrolyzes lactose into the monosaccharides
    glucose and galactose

60
LACTOSE INTOLERANCE
  • Production of insufficient amounts of lactase
    results in lactose intolerance
  • Lactose intolerance is due to lactase
    insufficiency
  • Various symptoms
  • Nausea, cramps, bloating, gas, diarrhea, etc.

X
61
LACTOSE INTOLERANCE
  • Lactose intolerance is the normal situation for
    adult humans
  • Lactase production generally begins to decline at
    about age 2
  • Lactase production generally halts by about age 4
  • Similar declines seen in other mammals
  • Such individuals become lactose intolerant

X
62
LACTOSE INTOLERANCE
  • The frequency of lactose intolerance varies
    widely throughout the world
  • Over 90 of humans overall
  • 4 of Swedes
  • 100 of individuals from certain African and
    Asian populations
  • Why do these rates differ so widely?

63
LACTOSE INTOLERANCE
  • Domestication of plants and animals began rather
    recently
  • Sheep, cattle, wheat, and barley were
    domesticated slightly over 10,000 years ago in
    the Near East
  • Profoundly altered the way people lived
  • Populations settled down and cultivated their
    own food
  • Populations began to grow
  • Cattle, sheep, grains, and lifestyle reached
    Western Europe a few millennia later

64
LACTOSE INTOLERANCE
  • Mutations causing lactase to be produced
    throughout adult life occurred in Western Europe
  • This mutation was beneficial in populations
    involved in intensive dairy farming
  • Natural selection increased its frequency in such
    populations
  • Lactose tolerance evolved in environments where
    milk is a major source of nutrition
  • A similar mutation also occurred in the Fulani
    people of Western Africa a couple thousand years
    ago

65
LACTOSE INTOLERANCE
  • Dairy farming was the cultural practice that
    drove the evolution of lactose tolerance
  • Highest levels of lactase deficiency in Asian
    populations not involved in dairy farming
  • Low levels of lactase deficiency in European
    populations with long histories of dairy farming
  • Low levels of lactase deficiency in West African
    populations relying extensively on milk in their
    diets

66
LACTOSE INTOLERANCE
  • Western Europeans colonized other areas of the
    world over the past five centuries
  • Gene conferring lactase traveled with them
  • Frequency of lactose tolerance increased in
    contacted populations

67
ROLES OF CARBOHYDRATES
  • Longer-term energy storage
  • Starch and glycogen are storage polysaccharides
  • Plants store excess sugars as starch
  • Animals store excess sugars as glycogen
  • Monosaccharides can be released via hydrolysis

68
ROLES OF CARBOHYDRATES
  • Structural roles
  • Cellulose is a major component of plant cell
    walls
  • Most abundant organic compound on earth
  • Polymer of glucose

69
ROLES OF CARBOHYDRATES
  • Structural roles
  • The covalent linkages between monomers differ
    between starch and cellulose
  • Different three-dimensional shapes
  • Linkages between starch monomers are easily
    hydrolyzed
  • Very few organisms can hydrolyze linkages
    between cellulose monomers
  • Lack the required enzymes

70
ROLES OF CARBOHYDRATES
  • Structural roles
  • Some microbes can digest cellulose
  • e.g., Cellulose-digesting bacteria in a cows
    rumen
  • e.g., Cellulose-digesting microbes in a termites
    gut
  • These relationships are examples of mutualism
  • Both organisms benefit from the interaction
  • How?

71
ROLES OF CARBOHYDRATES
  • Structural roles
  • Chitin is a major component of fungal cell walls
    and arthropod exoskeletons
  • Hardened with calcium carbonate in arthropods
  • Structure similar to cellulose

72
ROLES OF CARBOHYDRATES
73
ROLES OF CARBOHYDRATES
  • Cell communication
  • Glycoproteins and glycolipids on cell surface

74
LIPIDS
  • Not polymers
  • Comprised almost exclusively of C and H
  • Nonpolar bonds ? no H-bonding
  • Generally interact poorly with water
  • Hydrophobic

75
LIPIDS
  • Key roles of lipids
  • Energy storage
  • Insulation
  • Membrane components
  • Cell communication

76
LIPIDS
  • Major classes of lipids
  • Fats and oils
  • Phospholipids
  • Steroids

77
LIPIDS
  • Fats and oils
  • Triacylglycerols or triglycerides
  • Not polymers
  • Assembled from smaller molecules through
    condensation reactions
  • Glycerol
  • Three fatty acids

78
LIPIDS
  • Fats and oils
  • Fatty acids contain long carbon skeletons
  • Generally 16 18 carbons
  • These carbon skeletons may contain only single
    bonds
  • Saturated
  • These skeletons may contain double bonds
  • Unsaturated
  • Polyunsaturated
  • Cause chain to bend

79
LIPIDS
  • Fats and oils
  • Saturated fats
  • Present in fatty meats, dairy products, coconut
    oil, etc.
  • Possess only single bonds in fatty acid tails
  • Molecules can pack together tightly
  • Solid at room temperature

80
LIPIDS
  • Fats and oils
  • Unsaturated fats (oils)
  • Present in most plant and fish oils, etc.
  • Possess double bonds in fatty acid tails
  • Molecules cannot pack together as tightly
  • Generally liquid at room temperature

81
LIPIDS
  • Phospholipids
  • Similar to fats
  • Glycerol
  • 2 fatty acids
  • Phosphate
  • (Inositol, choline, etc.)
  • Amphipathic
  • Hydrophilic region
  • Hydrophobic region

82
LIPIDS
  • Phospholipids
  • Aggregate in water-rich environments
  • Micelles
  • Phospholipid bilayers
  • Key components of cell membranes
  • Hydrophobic regions are hidden from water
  • Hydrophilic regions are in contact with water

83
LIPIDS
  • Cholesterol
  • Steroid
  • Amphipathic
  • Membrane antifreeze
  • Prevents membrane solidification at low
    temperatures
  • Precursor for all steroid hormones

84
LIPIDS
  • Steroid hormones
  • Synthesized from cholesterol
  • Involved in a variety of body functions
  • e.g., Development
  • e.g., Reproduction
  • e.g., Salt regulation
  • e.g., Sugar biosynthesis
  • e.g., Water regulation
  • etc.

85
LIPIDS
86
PROTEINS
  • Comprise over 50 of dry mass of most cells
  • Very diverse in structure and function
  • Consist of one or more polypeptides
  • Polypeptides are chains of amino acids

87
PROTEINS
  • Proteins are polymers of amino acids
  • 20 different amino acids
  • Different R groups
  • Some hydrophilic
  • Some hydrophobic

88
PROTEINS
  • Amino acids are linked via condensation reactions
  • Amino acid of one reacts with the acid group of
    another
  • Form covalent peptide bonds
  • All proteins are made by assembling the same 20
    amino acids in different orders to different
    lengths

89
PROTEINS
  • Humans can make tens of thousands of distinctly
    different proteins
  • All use the same 20 amino acids
  • Different orders
  • Different lengths
  • How many distinctly different tripeptides can be
    assembled from these 20 amino acids?
  • tetrapeptides?

90
ESSENTIAL NONESSENTIAL
  • All organisms require all 20 amino acids
  • Humans can manufacture only ten of these amino
    acids from precursor molecules
  • Non-essential amino acids
  • Humans cannot manufacture the other ten amino
    acids
  • Essential amino acids
  • Must be acquired from diet
  • The bacterium Escherichia coli can manufacture
    all twenty amino acids
  • All amino acids are nonessential for E. coli
  • Humans can produce 12 amino acids from
    precursor molecules, but the precursor molecules
    for the production of two of these 12 amino acids
    are themselves essential amino acids (met ? cys,
    phe ? tyr)

91
ROLES OF PROTEINS
  • Key roles of proteins
  • Structural
  • Movement
  • Transport
  • Chemical messengers
  • Receptors
  • Storage
  • Defensive
  • Enzymes

92
ROLES OF PROTEINS
  • Hormones are one group of proteins
  • Chemical messengers involved in numerous
    processes
  • e.g., Insulin, glucagon, growth hormone, etc.
  • Remember, not all hormones are proteins
  • Steroid hormones are lipids
  • Other hormones are proteins

93
ROLES OF PROTEINS
  • Enzymes are biological catalysts
  • One important class of proteins
  • Speed up the rate of chemical reactions
  • Perhaps 10,000 times faster
  • Not consumed in this reactions
  • Highly specific

94
PROTEIN CONFORMATION
  • Each protein folds up into a particular
    three-dimensional shape
  • Protein function is related to its structure

95
PROTEIN CONFORMATION
  • Each protein folds up into a particular
    three-dimensional shape
  • Four levels of protein organization are
    recognized
  • Primary (1o) structure
  • Secondary (2o) structure
  • Tertiary (3o) structure
  • Quaternary (4o) structure

96
PROTEIN CONFORMATION
  • Primary structure
  • Linear sequence of amino acids
  • Genetically determined
  • Ultimately determines higher structural levels
  • The primary structure of the enzyme lysozyme is
    depicted
  • 129 amino acids long

97
PROTEIN CONFORMATION
  • Some regions of the polypeptide exhibit secondary
    structure
  • Formed by H-bonding at regular intervals along
    the polypeptide backbone
  • Two common types of secondary structure
  • Alpha-helices
  • Beta-pleated sheets

98
PROTEIN CONFORMATION
  • Tertiary structure involve interactions among
    R-groups
  • Four main factors
  • Hydrogen bonds
  • Ionic attractions
  • Hydrophobic interactions
  • Covalent bonds
  • Disulfide bridges

99
PROTEIN CONFORMATION
  • Quaternary structure results from interactions
    between multiple polypeptide chains
  • Not all proteins possess multiple polypeptide
    chains
  • Not all proteins possess quaternary structure

100
PROTEIN CONFORMATION
101
PROTEIN CONFORMATION
  • The three-dimensional conformation of a protein
    is critical to its function
  • Form determines function
  • Altered conformation can compromise function
  • Altered structure at any level can alter the
    final conformation
  • Altered chemical bonds can alter conformation

102
MUTATION CONFORMATION
  • The primary structure of a polypeptide is
    genetically determined
  • Primary structure ultimately determines the final
    shape of a protein
  • Mutations can alter the DNA sequence of a gene
  • Can alter the primary structure of the
    polypeptide
  • Can result in an altered three-dimensional shape
  • Basis of many genetic disorders

103
PROTEIN DENATURATION
  • Proteins can be denatured by a variety of factors
  • Temperature
  • pH
  • etc.
  • Denaturation alters the conformation of the
    protein
  • Often irreversible
  • It is difficult to un-hard-boil an egg

104
NUCLEIC ACIDS
  • Two classes of nucleic acids are found in cells
  • Deoxyribonucleic acid
  • DNA
  • Ribonucleic acid
  • RNA
  • Many of the functions of these nucleic acids are
    related or overlapping

105
NUCLEIC ACIDS
  • DNA
  • Polymer of deoxynucleotides
  • Genetic material of all cellular life and of some
    viruses
  • Organized into genes
  • Blueprints for proteins
  • RNA
  • Polymer of nucleotides
  • Genetic material of some viruses
  • Intermediates in gene expression
  • Ribosome components
  • Some possess enzyme-like activity
  • Ribozymes

106
(DEOXY)RIBONUCLEOTIDES
  • Nucleic acids are polymers
  • DNA monomers are deoxyribonucleotides
  • RNA monomers are ribonucleotides

107
(DEOXY)RIBONUCLEOTIDES
  • Nucleic acid monomers consist of three parts
  • Sugar
  • Nitrogenous base
  • Phosphate group(s)
  • These three parts are assembled by condensation
    reactions

108
(DEOXY)RIBONUCLEOTIDES
  • Both DNA and RNA possess a pentose sugar
  • Ribose in RNA
  • Deoxyribose in DNA
  • Lacks the 2 OH group possessed by ribose

?
109
(DEOXY)RIBONUCLEOTIDES
  • Both DNA and RNA possess four nitrogenous bases
  • Guanine
  • Adenine
  • Cytosine
  • Thymine (in DNA)
  • Uracil (in RNA)

110
(DEOXY)RIBONUCLEOTIDES
  • One or more phosphate groups are attached to the
    5 carbon of (deoxy)ribose
  • Triphosphates used in polynucleotide synthesis
  • Only one is incorporated into a DNA or RNA
    chain

111
(DEOXY)RIBONUCLEOTIDES
  • Some ribonucleotides have additional functions
  • e.g., ATP is involved in energy transfers
    within cells

112
POLYNUCLEOTIDES
  • Nucleotides are joined via condensation reactions
  • 3 OH and 5 phosphate OH
  • New nucleotides are added to the 3 end of
    growing chain
  • Two strands of double-stranded polynucleotides
    are NOT covalently linked
  • Interact through H-bonds

113
POLYNUCLEOTIDES
  • Structure of a single strand of DNA or RNA
  • Backbone of alternating sugar and phosphate
    groups
  • Nitrogenous bases projecting from this backbone

114
POLYNUCLEOTIDES
  • Most DNA and some RNA is double-stranded
  • Bases project from the sugar-phosphate backbone
  • Bases of two strands interact through H-bonds

115
POLYNUCLEOTIDES
  • DNA is organized into units called genes
  • A gene is a blueprint for a protein
  • RNA is an intermediate in gene expression
  • DNA ? RNA ? protein

116
ORIGIN OF LIFE
  • Life on Earth initially arose amidst a sea of
    various biological molecules
  • e.g., Amino acids, sugars, purines, ATP, etc.
  • The production and accumulation of these
    biological molecules preceded the origin of life
    on Earth

117
ORIGIN OF LIFE
  • Stanley Miller and Harold Urey recreated the
    assumed early atmosphere (1953)
  • Contained H2O, H2, CH4, and NH3
  • Lacked free O2
  • Energy input in forms of heat and electrical
    sparks
  • Mimic geothermal heat and lightning

118
ORIGIN OF LIFE
  • The initial Miller-Urey experiment and various
    similar experiments succeeded in producing
  • All 20 amino acids
  • Several sugars
  • Lipids
  • Purines and pyrimidines
  • ATP (when phosphate was added)
  • etc.

119
ORIGIN OF LIFE
  • The atmosphere replicated in these experiments
    likely differed from the earths early atmosphere
  • Atmosphere likely possessed little or no O2
  • Atmosphere likely possessed more CO, CO2, and N2
    than that in Millers experiment
  • Still, the Miller-Urey experiment did demonstrate
    that key organic molecules critical to life could
    be produced abiotically from inorganic precursors

120
ORIGIN OF LIFE
  • Other researchers have used combinations of gases
    based on our current understanding of Earths
    early atmosphere
  • Similar results were achieved
  • Organic molecules can be abiotically produced in
    an atmosphere composed primarily of H2O, CO, CO2,
    and N2

121
APPENDIX
  • CLASSES OF PROTEINS

122
ROLES OF PROTEINS
  • Structural proteins
  • e.g., Collagen, elastin, keratin, etc.

123
ROLES OF PROTEINS
  • Proteins facilitating movement
  • e.g., Actin, myosin, tubulin, etc.

124
ROLES OF PROTEINS
  • Transport proteins
  • e.g., Hemoglobin, lac permease, etc.

125
ROLES OF PROTEINS
  • Chemical messengers
  • e.g., Hormones and neurotransmitters
  • Receptors
  • Respond to chemical messengers

126
ROLES OF PROTEINS
  • Storage
  • e.g., Casein, ovalbumin, etc.

127
ROLES OF PROTEINS
  • Defensive
  • e.g., Antibodies, fibrin, etc.

128
ROLES OF PROTEINS
  • Enzymes
  • Highly specific catalysts of chemical reactions

129
REFERENCES
  • Campbell, Neil A. and Reese, Jane B. Biology,
    7th edition. Pearson Education, Inc. 2005.
  • Campbell, Neil A., Reese, Jane B., Taylor, Martha
    R., and Simon, Eric J. Biology, Concepts and
    Connections, 5th edition. Pearson Education,
    Inc. 2006.
  • Nester, Eugene W., Anderson, Denise G., Roberts,
    C. Evans Jr., and Nester, Martha T.
    Microbiology, A Human Perspective, 5th edition.
    McGraw-Hill Companies, Inc. 2007.
  • Limson, Janice. 2002. http//www.scienceinafrica
    .co.za/2002/june/lactose.htm
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