1. Ch. 5 Warm-Up Activity
1. What are the 4 biologically important organic
compounds, their building blocks and an
example of each?
2. What is the difference between dehydration
synthesis and hydrolysis? When are each used?
3. What are the 4 structural levels of a protein
and what bonds are involved in each?
4. What does it mean when a protein has been
denatured? What are some possible causes for
this to happen?
3. You Must Know
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The role of dehydration synthesis in the formation
of organic compounds and hydrolysis in the
digestion of organic compounds.
How to recognize the 4 biologically important organic
compounds (carbs, lipids, proteins, nucleic acids) by
their structural formulas.
The cellular functions of all four organic compounds.
The 4 structural levels of proteins
How proteins reach their final shape (conformation)
and the denaturing impact that heat and pH can
have on protein structure
4. Monomers
•Small organic
•Used for building
blocks of polymers
•Connects with
condensation reaction
(dehydration reaction)
Polymers
Macromolecules
•Long molecules of
•Giant molecules
monomers
•2 or more polymers
•With many identical or bonded together
similar blocks linked by
covalent bonds
ie. amino acid peptide polypeptide protein
smaller
larger
7. I. Carbohydrates
• Fuel and building material
• Include simple sugars (fructose) and polymers (starch)
• Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O
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monosaccharide disaccharide polysaccharide
Monosaccharides = monomers (ie. glucose, ribose)
Polysaccharides:
Differ in
Storage (plants-starch, animals-glycogen)
Structure (plant-cellulose, arthropod-chitin)
position &
orientation of
glycosidic
linkage
13. II. Lipids
A. Fats (triglyceride): store large amounts
of energy (2x carbohydrates), cushions
organs and insulates body
Glycerol + 3 Fatty Acids
saturated, unsaturated, polyunsaturated
A. Steroids: cholesterol and hormones
Steroids
B. Phospholipids: cell membrane
hydrophilic head, hydrophobic tails
creates bilayer to form cell membrane
Hydrophilic head
Hydrophobic tail
22. III. Proteins
Four Levels of Protein Structure:
1. Primary
Amino acid (AA) sequence
20 different AA’s
peptide bonds link AA’s
23. Four Levels of Protein Structure (continued)
2. Secondary
Gains 3-D shape (folds, coils) by H-bonding
Alpha (α) helix, Beta (β) pleated sheet
24. Four Levels of Protein Structure (continued)
3. Tertiary
Bonding between side chains (R groups) of amino acids
H & ionic bonds, disulfide bridges, van der Waals
interactions
25. Four Levels of Protein Structure (continued)
4. Quaternary
2+ polypeptides bond together
26. amino acids polypeptides protein
Bonding (ionic & H) can create
asymmetrical attractions
30. IV. Nucleic Acids
Function: carry hereditary info
DNA
•Double stranded helix
• N-bases: A, G, C, Thymine
•Stores hereditary info
•Longer/larger
•Sugar: deoxyribose
RNA
•Single stranded
• N-bases: A, G, C, Uracil
•Carry info from DNA to
ribosomes
•tRNA, rRNA, mRNA,
RNAi
•Sugar: ribose
31. Nucleotides: monomer of DNA/RNA
3 parts:
-nitrogen base
-pentose sugar
-ribose
-deoxyribose
-P04 group
35. Nucleic polymer
• Backbone
Sugar to PO4 bond
Phosphodiester bond
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new base added to sugar of previous base
Polymer grow in one direction
N bases hang off the sugar-phosphate
backbone
36. Pairing of nucleotides
• Nucleotides bond between DNA strands
H bonds
Purine :: Pyrimidine
A :: T
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2 H bonds
G :: C
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3 H bonds
37. DNA RNA protein:
a diagrammatic overview
of information flow in a
cell.