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Carbon Chemistry
Macromolecules
Carbon
 Carbon—The Backbone of
Biological Molecules
 All living organisms are
made up of chemicals
based mostly on the
element carbon
 Carbon Chains & Rings
ETC
 skeletons of most organic
molecules
Importance of Carbon
 70 to 95% of cells are water
 Carbon makes up the rest of the compounds.
 2/3 of our dry weight (mostly proteins)
 Organic compounds can range from the
simple (CO2 or CH4) to complex molecules,
like proteins.
 While the percentages of major elements do
not vary within or amongst species, variations
in organic molecules can distinguish even
between individuals of a single species.
Some Common Carbon Compounds
Isomers
 Isomers
 Are molecules with the same molecular
formula but different structures and
properties
 Three types of isomers are
 Structural
 Geometric
 Enantiomers
H H H H H
H
H H H H H
H
H
H
H
H
H
H
H
H
H
H
H
H
H
H
H
H
CO2H
CH3
NH2
C
CO2H
H
CH3
NH2
X X
X
X
C C C C C
C
C
C C C
C C C C
C
(a) Structural isomers
(b) Geometric isomers
(c) Enantiomers
See fig 4.8 pg 63
H
Intro. Cont………
 Combinations of carbon and hydrogen form
hydrocarbons, many of which we use:
Gasoline propane ect….
 Organic compounds also form biological
molecules: Macromolecules. Ex.
Carbohydrates, lipids, proteins, and nucleic
acids.
 These macromolecules are made from simple
sugars, amino acids, nucleotides, and fatty
acids.
Functional Groups of Carbon compounds.
 Functional groups
 The number and arrangement of functional
groups help give each molecule its distinctive
properties
 There are 7 functional groups that are
important to the chemistry of life: hydroxyl,
carbonyl, carboxyl, amino, sulfhydryl, methyl,
and phosphate groups.
Functional Group Example
Hydroxyl Group
 In a hydroxyl group (-OH)
 Free radical
Carbonyl Group
 A carbonyl group (=CO)
 end of the skeleton = aldelhyde.
 If not, then the compound is a ketone.
Carboxyl group
 A carboxyl group (-COOH)
 Carboxylic acids
Amino Group
 An amino group (-NH2)
 Amines are organic compounds with amino groups
Amino acids, the building blocks of proteins, have amino
and carboxyl groups.
 A sulfhydryl group (-SH)
 Sulfhydryl groups help stabilize the structure of
proteins.
Sulfhydryl group
Phosphate group
 A phosphate group (-OPO3
2-) consists of phosphorus
bound to four oxygen atoms (three with single bonds and
one with a double bond).
 Ex. ATP
Macromolecules Introduction
 Cells join small molecules to form large
molecules.
 Macromolecules, thousands of atoms and
weigh over 100,000 daltons.
 The four major classes of macromolecules are:
carbohydrates, lipids, proteins, and nucleic
acids
 They have very complex structures esp.
proteins
The Synthesis and Breakdown of
Polymers
 Condensation or dehydration synthesis
reactions
(a) Dehydration reaction in the synthesis of a polymer
HO H
1 2 3 HO
HO H
1 2 3 4
H
H2O
Short polymer Unlinked monomer
Longer polymer
Dehydration removes a water
molecule, forming a new bond
 Polymers can disassemble by
 Hydrolysis
(b) Hydrolysis of a polymer
HO 1 2 3 H
HO H
1 2 3 4
H2O
H
HO
Hydrolysis adds a water
molecule, breaking a bond
Figure 5.2B
Carbohydrates
 Carbohydrates or sugars can be simple or
complex.
 Simple sugars are called Monosaccharides.
 Disaccharides
 Polysaccharides
 Carbs. Are the most numerous molecules in
life.
Monosaccharides
 CH2O.
 Ex. Glucose,
Ribose
Disaccharides
Polysaccharides
 Polysaccharides hundreds to thousands of
monosaccharides joined by glycosidic linkages
 One function is to store energy or serve as
building materials for the cell or whole organism.
 Starch composed entirely of glucose monomers.
(plants)
 Animals too store glucose glycogen.
All about Shape
Cont.
 Chitin, another important structural
polysaccharide
O
CH2O
H
OH
H
H OH
H
NH
C
CH3
O
H
H
(b) Chitin forms the exoskeleton
of arthropods.
(c) Chitin is used to make a
strong and flexible surgical
thread that decomposes
after
the wound or incision heals.
OH
Figure 5.10 A–C
Lipids or FATS
 Hydrophobic
 Lipids have 1-3 fatty acids attached to a glycerol
molecule.
 There are saturated and unsaturated fats. Saturated
fats have double bond and unsaturated do not.
 Triglycerides -energy source.
 Phospholipids
 Sterols- they have no fatty acids. Ex. Cholesterol
Phospholipid Bilayer
Proteins
 Proteins are influential in about everything
 Functions include storage, structural support,
transport of other substances, intercellular
signaling, movement, and defense against foreign
substances.
 Enzymes
 Humans have an estimated 200,000 various
proteins,
 Most structurally complex molecules known.
 Polymers of amino acids
Modeling Protein Stucture
Figure 5.1
Amino Acids
Amino Acid Polymers
 Peptide bonds OH
DESMOSOMES
DESMOSOMES
DESMOSOMES
OH
CH2
C
N
H
C
H O
H OH OH
Peptide
bond
OH
OH
OH
H H
H
H
H
H
H
H
H
H H
H
N
N N
N N
SH Side chains
SH
O
O
O O O
H2O
CH2 CH2
CH2 CH2 CH2
C C C C C C
C C
C C
Peptide
bond
Amino end
(N-terminus)
Backbone
(a)
Figure 5.18 (b)
Carboxyl end
(C-terminus)
Function of Proteins
 depends on shape.
 function depends on its capacity to recognize and bind to some
other molecule.
 AB, Enzymes, and NT all based on shape
An overview of protein functions
Structure ( See pg 82-84)
 Chaperonins
 Are protein molecules that assist in the proper
folding of other proteins
Hollow
cylinder
Cap
Chaperonin
(fully assembled)
Steps of Chaperonin
Action:
An unfolded poly-
peptide enters the
cylinder from one end.
The cap attaches, causing
the cylinder to change shape in
such a way that it creates a
hydrophilic environment for the
folding of the polypeptide.
The cap comes
off, and the properly
folded protein is
released.
Correctly
folded
protein
Polypeptide
2
1
3
Figure 5.23
Protein structure can change
 Changes.
 pH, salt
concentration,
temperature, or
other factors
can unravel or
denature a
protein
 mutation Pg 48
How do we Know
 X-ray crystallography helps determine protein
conformation.
 This technique requires the formation of a crystal
of the protein being studied.
 The pattern of diffraction of an X-ray by the atoms
of the crystal can be used to determine the location
of the atoms and to build a computer model of its
structure.
The Instructions for Life Nucleic Acids
There are two types of nucleic acids: ribonucleic
acid (RNA) and deoxyribonucleic acid (DNA).
 DNA gives direction for its own replication,
repair, and control.
 DNA also directs RNA synthesis and through
RNA, controls protein synthesis.
 Organisms inherit DNA from their parents.
Nucleic Acids
 Nucleic acids are many nucleotides joined
together.
 Each nucleotide consists of three parts: a
nitrogen base, a pentose, 5 carbon, sugar, and a
phosphate group
 Pyrimidines have a single six-membered ring.
 CTU
 Purine have a six-membered ring joined to a five-
membered ring. So have 2 rings not 1
 AG
Carbon_Chemistry slides for chemistry of science
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Carbon_Chemistry slides for chemistry of science

  • 2. Carbon  Carbon—The Backbone of Biological Molecules  All living organisms are made up of chemicals based mostly on the element carbon  Carbon Chains & Rings ETC  skeletons of most organic molecules
  • 3. Importance of Carbon  70 to 95% of cells are water  Carbon makes up the rest of the compounds.  2/3 of our dry weight (mostly proteins)  Organic compounds can range from the simple (CO2 or CH4) to complex molecules, like proteins.  While the percentages of major elements do not vary within or amongst species, variations in organic molecules can distinguish even between individuals of a single species.
  • 4. Some Common Carbon Compounds
  • 5. Isomers  Isomers  Are molecules with the same molecular formula but different structures and properties  Three types of isomers are  Structural  Geometric  Enantiomers
  • 6. H H H H H H H H H H H H H H H H H H H H H H H H H H H H CO2H CH3 NH2 C CO2H H CH3 NH2 X X X X C C C C C C C C C C C C C C C (a) Structural isomers (b) Geometric isomers (c) Enantiomers See fig 4.8 pg 63 H
  • 7. Intro. Cont………  Combinations of carbon and hydrogen form hydrocarbons, many of which we use: Gasoline propane ect….  Organic compounds also form biological molecules: Macromolecules. Ex. Carbohydrates, lipids, proteins, and nucleic acids.  These macromolecules are made from simple sugars, amino acids, nucleotides, and fatty acids.
  • 8. Functional Groups of Carbon compounds.  Functional groups  The number and arrangement of functional groups help give each molecule its distinctive properties  There are 7 functional groups that are important to the chemistry of life: hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, methyl, and phosphate groups.
  • 10. Hydroxyl Group  In a hydroxyl group (-OH)  Free radical
  • 11. Carbonyl Group  A carbonyl group (=CO)  end of the skeleton = aldelhyde.  If not, then the compound is a ketone.
  • 12. Carboxyl group  A carboxyl group (-COOH)  Carboxylic acids
  • 13. Amino Group  An amino group (-NH2)  Amines are organic compounds with amino groups Amino acids, the building blocks of proteins, have amino and carboxyl groups.
  • 14.  A sulfhydryl group (-SH)  Sulfhydryl groups help stabilize the structure of proteins. Sulfhydryl group
  • 15. Phosphate group  A phosphate group (-OPO3 2-) consists of phosphorus bound to four oxygen atoms (three with single bonds and one with a double bond).  Ex. ATP
  • 16. Macromolecules Introduction  Cells join small molecules to form large molecules.  Macromolecules, thousands of atoms and weigh over 100,000 daltons.  The four major classes of macromolecules are: carbohydrates, lipids, proteins, and nucleic acids  They have very complex structures esp. proteins
  • 17. The Synthesis and Breakdown of Polymers  Condensation or dehydration synthesis reactions (a) Dehydration reaction in the synthesis of a polymer HO H 1 2 3 HO HO H 1 2 3 4 H H2O Short polymer Unlinked monomer Longer polymer Dehydration removes a water molecule, forming a new bond
  • 18.  Polymers can disassemble by  Hydrolysis (b) Hydrolysis of a polymer HO 1 2 3 H HO H 1 2 3 4 H2O H HO Hydrolysis adds a water molecule, breaking a bond Figure 5.2B
  • 19. Carbohydrates  Carbohydrates or sugars can be simple or complex.  Simple sugars are called Monosaccharides.  Disaccharides  Polysaccharides  Carbs. Are the most numerous molecules in life.
  • 22. Polysaccharides  Polysaccharides hundreds to thousands of monosaccharides joined by glycosidic linkages  One function is to store energy or serve as building materials for the cell or whole organism.  Starch composed entirely of glucose monomers. (plants)  Animals too store glucose glycogen.
  • 24. Cont.
  • 25.  Chitin, another important structural polysaccharide O CH2O H OH H H OH H NH C CH3 O H H (b) Chitin forms the exoskeleton of arthropods. (c) Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals. OH Figure 5.10 A–C
  • 26. Lipids or FATS  Hydrophobic  Lipids have 1-3 fatty acids attached to a glycerol molecule.  There are saturated and unsaturated fats. Saturated fats have double bond and unsaturated do not.  Triglycerides -energy source.  Phospholipids  Sterols- they have no fatty acids. Ex. Cholesterol
  • 27.
  • 29. Proteins  Proteins are influential in about everything  Functions include storage, structural support, transport of other substances, intercellular signaling, movement, and defense against foreign substances.  Enzymes  Humans have an estimated 200,000 various proteins,  Most structurally complex molecules known.  Polymers of amino acids
  • 32. Amino Acid Polymers  Peptide bonds OH DESMOSOMES DESMOSOMES DESMOSOMES OH CH2 C N H C H O H OH OH Peptide bond OH OH OH H H H H H H H H H H H H N N N N N SH Side chains SH O O O O O H2O CH2 CH2 CH2 CH2 CH2 C C C C C C C C C C Peptide bond Amino end (N-terminus) Backbone (a) Figure 5.18 (b) Carboxyl end (C-terminus)
  • 33. Function of Proteins  depends on shape.  function depends on its capacity to recognize and bind to some other molecule.  AB, Enzymes, and NT all based on shape
  • 34. An overview of protein functions
  • 35. Structure ( See pg 82-84)
  • 36.  Chaperonins  Are protein molecules that assist in the proper folding of other proteins Hollow cylinder Cap Chaperonin (fully assembled) Steps of Chaperonin Action: An unfolded poly- peptide enters the cylinder from one end. The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide. The cap comes off, and the properly folded protein is released. Correctly folded protein Polypeptide 2 1 3 Figure 5.23
  • 37. Protein structure can change  Changes.  pH, salt concentration, temperature, or other factors can unravel or denature a protein  mutation Pg 48
  • 38. How do we Know  X-ray crystallography helps determine protein conformation.  This technique requires the formation of a crystal of the protein being studied.  The pattern of diffraction of an X-ray by the atoms of the crystal can be used to determine the location of the atoms and to build a computer model of its structure.
  • 39.
  • 40. The Instructions for Life Nucleic Acids There are two types of nucleic acids: ribonucleic acid (RNA) and deoxyribonucleic acid (DNA).  DNA gives direction for its own replication, repair, and control.  DNA also directs RNA synthesis and through RNA, controls protein synthesis.  Organisms inherit DNA from their parents.
  • 41. Nucleic Acids  Nucleic acids are many nucleotides joined together.  Each nucleotide consists of three parts: a nitrogen base, a pentose, 5 carbon, sugar, and a phosphate group  Pyrimidines have a single six-membered ring.  CTU  Purine have a six-membered ring joined to a five- membered ring. So have 2 rings not 1  AG