Download Midterm Review Project Ch 5

Chapter 5 Review Sheet: The Structure and Function of Large Biological Molecules
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Macromolecule= polymer made from monomers
dehydration reaction: water molecule lost, bond forms
hydrolysis: water added, bond broken
Carbohydrates
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monosaccharide (simplest carbohydrates/simple sugars), 2 of which make a disaccharide joined by a glycosidic linkage
(covalent bond formed by a dehydration reaction: either alpha or beta linkage depending on location of hydroxyl group in
glucose monomers), then polysaccharides if multiple monosaccharides
polysaccharides’ function: storage material hydrolyzed for sugar, building material for structures that protect the
cell/organism
o storage: plants have starch, animals have glycogen- both polymers of glucose
o structural: cellulose in plants (most abundant organic compound)- beta linkage so enzymes that digest other starches
can’t necessarily digest cellulose
Lipids
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not polymers, but fat is made from glycerol- 3 carbons, each bearing a hydroxyl
group-and fatty acids- carboxyl group attached to a hydrocarbon chain
nonpolar hydrocarbon bond make fats hydrophobic
saturated fatty acid:solid at room temp, saturated with hydrogen; unsaturated fatty
acid: liquid at room temp., double bonds by removal of hydrogen atoms from carbon
skeleton
phospholipids make cell membrance: hydrophilic head on outside and
hydrophobic tail on inside of bilayer
steroids, cholesterol
Polypeptides
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proteins can be enzymes: catalysts, chemical agents that selectively speed up chemical
reactions without being consumed by the reaction
monomers: amino acids that make polypeptides, protein: one or more polypeptides
amino acid: amino group, carboxyl group, an alpha carbon and an R group, the variable
group that differentiates amino acids (the group’s properties, whether it is polar or not,
determine if amino acid is hydrophilic or not)
primary structure: amino acid sequence; secondary structure: coils and folds as a result of hydrogen bonds, alpha- helix,
beta-pleated sheet; tertiary structure: overall shape of polypeptide created by hydrophobic interaction ( hydrophobic side
chains end up at core of protein) and disulfide bridges; quaternary structure: overall protein structure from the
polypeptide subunits (two or more polypeptide chains)
proteins can denature (primary structure doesn’t change unless genetically): high temps, various chem. treatments: it
loses its shape and its ability to function, sometimes can renature if environment is restored to normal
peptide bonds between amino acids
Nucleic Acids
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DNA- double stranded- deoxyribose sugar , RNA- single stranded- ribose sugar: both
genetic material, controls protein synthesis
monomer: nucleotides- bases are pyrimidines C,T,U; purines A,G
o 3 parts of nucleotides are the phosphate group, 5 carbon sugar, nitrogenous
base
DNA: complementary strands: A-T (or U in RNA), C-G; 5’ on one end, 3’ on other and
reverse for complementary strand