Chapter 3 The Chemistry of Organic Molecules AP Biology.
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Transcript of Chapter 3 The Chemistry of Organic Molecules AP Biology.
![Page 1: Chapter 3 The Chemistry of Organic Molecules AP Biology.](https://reader035.fdocuments.in/reader035/viewer/2022081512/56649d815503460f94a65cd5/html5/thumbnails/1.jpg)
Chapter 3The Chemistry of Organic Molecules
AP Biology
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Definitions
• Organic Molecules– Bonding of H, O, N, and other molecules to
carbon.– Characterize the structure and function of living
things
• Inorganic Molecules– Do not contain C and H together– Nonliving matter; however they play important
roles in living things
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Functional Groups
• Functional groups are the parts of molecules involved in chemical reactions
• Give organic molecules distinctive chemical properties (ex. Polarity, hydophobic/philic, acidic, etc.)
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• Six functional groups are important in the chemistry of life: (see Figure 3.2, pg 35)– Hydroxyl – Carbonyl – Carboxyl– Amino– Sulfhydryl– Phosphate
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Isomers
• Isomers are molecules with the same molecular formula but different structures (different functional groups) and properties
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Macromolecules
– Are large molecules composed of smaller molecules
– Are complex in their structures
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Macromolecules
•Macromolecules are polymers, built from monomers• Four classes of life’s organic molecules are polymers– Carbohydrates– Proteins– Nucleic acids– Lipids
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The Synthesis and Breakdown of Polymers
• Monomers form larger molecules by condensation reactions called dehydration synthesis
(a) Dehydration reaction in the synthesis of a polymer
HO H1 2 3 HO
HO H1 2 3 4
H
H2O
Short polymer Unlinked monomer
Longer polymer
Dehydration removes a watermolecule, forming a new bond
Figure 5.2A
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The Synthesis and Breakdown of Polymers
• Polymers can disassemble by– Hydrolysis (addition of water molecules)
(b) Hydrolysis of a polymer
HO 1 2 3 H
HO H1 2 3 4
H2O
HHO
Hydrolysis adds a watermolecule, breaking a bond
Figure 5.2B
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Carbohydrates• Monosaccharides
– Glucose– Fructose– Ribose/Deoxyribose
• Disaccharides– Lactose– Maltose– Sucrose
• Polysaccharides– Starch– Glycogen– Cellulose– Chitin
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Lipids• Lipids are a diverse group of hydrophobic
molecules (nonpolar and insoluble)• Lipids– Are the one class of large biological
molecules that do not consist of polymers– Provide energy storage– Act as cell messengers
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Fats– Are constructed from two types of smaller molecules, a
single glycerol and usually three fatty acids– Vary in the length and number and locations of double
bonds they contain
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• Saturated fatty acids– Have the maximum number of hydrogen
atoms possible– Have no double bonds
(a) Saturated fat and fatty acid
Stearic acid
Figure 5.12
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• Unsaturated fatty acids– Have one or more double bonds
(b) Unsaturated fat and fatty acidcis double bondcauses bending
Oleic acid
Figure 5.12
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Waxes
• Chains of fatty acids bonded to an alcohol chain.
• Solid• Protective
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• Phospholipids– Have only two fatty acids– Have a phosphate group instead of a third
fatty acid
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• Phospholipid structure–Consists of a hydrophilic “head” and
hydrophobic “tails”CH2
O
PO O
O
CH2CHCH2
OO
C O C O
Phosphate
Glycerol
(a) Structural formula (b) Space-filling model
Fatty acids
(c) Phospholipid symbol
Hyd
rop
hob
i c t
ails
Hydrophilichead
Hydrophobictails
–
Hyd
rop
hi li c
head
CH2 Choline+
Figure 5.13
N(CH3)3
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• The structure of phospholipids– Results in a bilayer arrangement found in cell
membranes
Hydrophilichead
WATER
WATER
Hydrophobictail
Figure 5.14
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Steroids
• Steroids– Are lipids characterized by a carbon skeleton
consisting of four fused rings– Differ with functional groups
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• One steroid, cholesterol– Is found in cell membranes– Is a precursor for some hormones
HO
CH3
CH3
H3C CH3
CH3
Figure 5.15
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Proteins
• Support• Enzymes• Transport• Defense• Hormones• Motion
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• Amino acids– Are organic molecules possessing both
carboxyl (acidic) and amino groups– Differ in their properties due to differing side
chains, called R groups
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Amino Acid Polymers
• Amino acids– Are linked by peptide bonds (covalent)
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Protein Structure
• A protein’s specific conformation (shape) determines how it functions
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Four Levels of Protein Structure
• Primary structure– Is the unique sequence
of amino acids in a polypeptide
Figure 5.20–
Amino acid
subunits
+H3NAmino
end
oCarboxyl end
oc
GlyProThrGlyThr
Gly
GluSeuLysCysProLeu
MetVal
Lys
ValLeu
AspAlaValArgGly
SerPro
Ala
Gly
lle
SerProPheHisGluHis
Ala
GluValValPheThrAla
Asn
AspSer
GlyProArg
ArgTyrThr
lleAla
Ala
Leu
LeuSer
ProTyrSerTyrSerThr
Thr
Ala
ValVal
ThrAsnProLysGlu
ThrLys
SerTyrTrpLysAlaLeu
GluLleAsp
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O C helix
pleated sheetAmino acid
subunitsNCH
C
O
C N
H
CO H
R
C NH
C
O H
C
R
N
HH
R C
O
R
C
H
NH
C
O H
NCO
R
C
H
NH
H
C
R
C
O
C
O
C
NH
H
R
C
C
ON
HH
C
R
C
O
NH
R
C
H C
ON
HH
C
R
C
O
NH
R
C
H C
ON
HH
C
R
C
O
N H
H C R
N HO
O C N
C
RC
H O
CHR
N HO C
RC
H
N H
O CH C R
N H
CC
N
R
H
O C
H C R
N H
O C
RC
H
H
C
RN
H
CO
C
NH
R
C
H C
O
N
H
C
• Secondary structure– Is the folding or coiling of the polypeptide into a
repeating configuration– Includes the helix and the pleated sheet
H H
Figure 5.20
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• Tertiary structure– Is the overall three-dimensional shape of a
polypeptide– Results from interactions between amino acids
and R groups
CH2CH
OH
O
CHO
CH2
CH2 NH3+ C-O CH2
O
CH2SSCH2
CH
CH3
CH3
H3C
H3C
Hydrophobic interactions and van der Waalsinteractions Polypeptid
ebackbone
Hyrdogenbond
Ionic bond
CH2
Disulfide bridge
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• Quaternary structure– Results when two or more polypeptide chains
combine.
Polypeptidechain
Collagen
Chains
ChainsHemoglobin
IronHeme
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Protein Structure
• http://www.stolaf.edu/people/giannini/
• http://www.stolaf.edu/people/giannini/flashanimat/proteins/protein%20structure.swf
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•Denaturation is when a protein unravels and loses its native conformation(shape) Denaturation
Renaturation
Denatured protein
Normal protein
Figure 5.22
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Nucleic Acids
• Made of nucleotide monomers
• Two Types: DNA & RNA– Differences in structure
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ATP
• A nucleotide of ribose and adenine• 5-C sugar and 3 phosphates• High energy (bonds)