Warm-Up 1.What are the 4 classes of macromolecules? 2.Give an example of each type of macromolecule.
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Transcript of Warm-Up 1.What are the 4 classes of macromolecules? 2.Give an example of each type of macromolecule.
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Warm-UpWarm-Up
1.1. What are the 4 classes of What are the 4 classes of macromolecules?macromolecules?
2.2. Give an example of each Give an example of each type of macromolecule.type of macromolecule.
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Ch. 5 Warm-Up ActivityCh. 5 Warm-Up Activity
In your family groups, In your family groups, complete #1-5 on Activity complete #1-5 on Activity
4/5.1: 4/5.1: ““How can you identify How can you identify organic macromolecules?organic macromolecules?””
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Warm-UpWarm-Up
1.1. What are the 4 levels of protein What are the 4 levels of protein structure? What bonds are formed structure? What bonds are formed in each level?in each level?
2.2. Which protein was involved in the Which protein was involved in the curds & whey lab yesterday?curds & whey lab yesterday?
3.3. Explain what happened to the milk Explain what happened to the milk to form the curds and whey.to form the curds and whey.
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Chapter 5Chapter 5
The Structure and The Structure and Function of Large Function of Large
Biological MoleculesBiological Molecules
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You Must KnowYou Must Know• The role of The role of dehydration synthesisdehydration synthesis in the in the
formation of organic compounds and formation of organic compounds and hydrolysishydrolysis in the digestion of organic compounds.in the digestion of organic compounds.
• How to recognize the 4 biologically important How to recognize the 4 biologically important organic compounds (carbs, lipids, proteins, organic compounds (carbs, lipids, proteins, nucleic acids) by their structural formulas.nucleic acids) by their structural formulas.
• The cellular functions of all four organic The cellular functions of all four organic compounds.compounds.
• The 4 structural levels of proteinsThe 4 structural levels of proteins• How proteins reach their final shape How proteins reach their final shape
((conformationconformation) and the ) and the denaturingdenaturing impact impact that heat and pH can have on protein structurethat heat and pH can have on protein structure
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Monomers PolymersMacromolec
ules•Small organic •Used for building blocks of polymers•Connects with condensation reaction (dehydration synthesis)
•Long molecules of monomers•With many identical or similar blocks linked by covalent bonds
•Giant molecules•2 or more polymers bonded together
ie. amino acid peptide polypeptide protein
smaller larger
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Dehydration Synthesis
(Condensation Reaction)
Hydrolysis
Make polymers Breakdown polymers
Monomers Polymers Polymers Monomers
A + B AB AB A + B
+ H2O
+ + H2O
+
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I. ProteinsI. Proteins• ““Proteios” = first or primaryProteios” = first or primary• 50% dry weight of cells50% dry weight of cells• Contains: C, H, O, N, SContains: C, H, O, N, S
Myoglobin protein
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Protein Functions (+ Protein Functions (+ examples)examples)• Enzymes (lactase)Enzymes (lactase)• Defense (antibodies)Defense (antibodies)• Storage (milk protein = casein)Storage (milk protein = casein)• Transport (hemoglobin)Transport (hemoglobin)• Hormones (insulin)Hormones (insulin)• ReceptorsReceptors• Movement (motor proteins)Movement (motor proteins)• Structure (keratin)Structure (keratin)
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Overview of protein Overview of protein functionsfunctions
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Overview of protein Overview of protein functionsfunctions
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Four Levels of Protein Four Levels of Protein StructureStructure1.1. PrimaryPrimary
Amino acid Amino acid (AA) sequence(AA) sequence 20 different AA’s20 different AA’s peptide bonds peptide bonds link AA’slink AA’s
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Amino AcidAmino Acid
• R group R group = side = side chainschains
• PropertiesProperties::• hydrophobichydrophobic• hydrophilichydrophilic• ionic (acids & ionic (acids &
bases)bases)
• ““amino” : -NHamino” : -NH22
• ““acid” : -COOHacid” : -COOH
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Four Levels of Protein Structure Four Levels of Protein Structure (continued)(continued)2.2. SecondarySecondary
Gains 3-D shape (folds, coils) by Gains 3-D shape (folds, coils) by H-H-bondingbonding
Alpha (α) helixAlpha (α) helix, , Beta (Beta (ββ) pleated ) pleated sheetsheet
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Four Levels of Protein Structure Four Levels of Protein Structure (continued)(continued)
3.3. TertiaryTertiary Bonding between Bonding between side chainsside chains (R groups) (R groups) of of
amino acidsamino acids H bonds, ionic bonds, disulfide bridges, van H bonds, ionic bonds, disulfide bridges, van
der Waals interactionsder Waals interactions
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Four Levels of Protein Structure Four Levels of Protein Structure (continued)(continued)4.4. QuaternaryQuaternary
2+ polypeptides 2+ polypeptides bond togetherbond together
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amino acids amino acids polypeptides polypeptides proteinprotein
Bonding (ionic & H) can create asymmetrical attractions
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ChaperoninsChaperonins assist in proper assist in proper folding of proteinsfolding of proteins
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• Protein Protein structure and function structure and function are sensitive to chemical and are sensitive to chemical and physical conditionsphysical conditions
• Unfolds or Unfolds or denaturesdenatures if if pHpH and and temperaturetemperature are not optimal are not optimal
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change in change in structurestructure = change = change in in functionfunction
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II. Nucleic AcidsII. Nucleic Acids
Function: store hereditary infoFunction: store hereditary info
DNA RNA• Double-stranded
helix• N-bases: A, G, C,
ThymineThymine• Stores hereditary
info• Longer/larger• Sugar: deoxyribose
• Single-stranded• N-bases: A, G, C,
UracilUracil• Carry info from
DNA to ribosomes• tRNA, rRNA,
mRNA, RNAi• Sugar: ribose
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NucleotidesNucleotides: monomer of : monomer of DNA/RNADNA/RNA
NucleotideNucleotide = = SugarSugar + + PhosphatePhosphate + + Nitrogen BaseNitrogen Base
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NucleotideNucleotidephospha
te
5-C sugar
Nitrogen base
A – TG – C
Purines Pyrimidines
•Adenine•Guanine
•Cytosine•Thymine (DNA)•Uracil (RNA)
•Double ring •Single ring
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Information flow in a cell:Information flow in a cell:DNA DNA RNA RNA protein protein
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III. CarbohydratesIII. Carbohydrates• FuelFuel and and building materialbuilding material• Include simple sugars (fructose) and polymers Include simple sugars (fructose) and polymers
(starch)(starch)
• Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CHRatio of 1 carbon: 2 hydrogen: 1 oxygen or CH22OO
• monosaccharidemonosaccharide disaccharidedisaccharide polysaccharidepolysaccharide• MonosaccharidesMonosaccharides = monomers (eg. glucose, = monomers (eg. glucose,
ribose)ribose)• PolysaccharidesPolysaccharides::
StorageStorage (plants-starch, animals-glycogen) (plants-starch, animals-glycogen) StructureStructure (plant-cellulose, arthropod-chitin (plant-cellulose, arthropod-chitin))
Differ in position & orientation
of glycosidic
linkage
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The structure The structure and and classification classification of some of some monosaccharidmonosaccharideses
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Linear and ring forms of Linear and ring forms of glucoseglucose
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Carbohydrate synthesisCarbohydrate synthesis
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Cellulose vs. StarchCellulose vs. Starch
Two Forms of Glucose: Two Forms of Glucose: glucose & glucose & glucoseglucose
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Cellulose vs. StarchCellulose vs. Starch• Starch = Starch = glucose monomers glucose monomers• Cellulose = Cellulose = glucose monomers glucose monomers
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Storage polysaccharides of Storage polysaccharides of plantsplants (starch) and (starch) and animalsanimals (glycogen) (glycogen)
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Structural polysaccharides: cellulose & chitin Structural polysaccharides: cellulose & chitin (exoskeleton)(exoskeleton)
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II. LipidsII. LipidsA.A. Fats (triglyceride): Fats (triglyceride): store energy
Glycerol + 3 Fatty Acids saturated, unsaturated,
polyunsaturated
B.B. SteroidsSteroids: cholesterol and hormones
C.C. Phospholipids: Phospholipids: lipid bilayer of lipid bilayer of cell membrane
hydrophilic head, hydrophobic tails
Hydrophilic headHydrophobic tail
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Saturated UnsaturatedPolyunsatura
ted“saturated” with H Have some C=C, result in kinks
In animals In plants
Solid at room temp.
Liquid at room temp.
Eg. butter, lard Eg. corn oil, olive oil
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Cholesterol, a steroid
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The structure of a phospholipid
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Hydrophobic/hydrophilic interactions make a phospholipid bilayer
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