AP Bio Chapter 5 Reading Guide Answers

The large molecules of all living things fall into just four main categories:
Carbohydrates, proteins, nucleic acids, lipids
Circle the three classes that are called macromolecules:
Carbohydrates, proteins, nucleic acids
What is a polymer?
Chain-like molecules consisting of many similar building blocks linked by covalent bonds.
What is a monomer?
The repeating units that serve as building blocks for polymers.
Monomers are connected in what type of reaction?
Dehydration synthesis–a bond forms between two monomers, each contributes part of a water molecule to be released.
Large molecules are converted to monomers in what type of reaction?
Hydrolysis–bond broken between monomers by addition of water.
Hydro-
water
-lysis
break
Is C6H12O6 (Glucose) a monomer, or a polymer?
Monomer
How are two monomers joined?
H2O released
What are the monomers of all carbohydrates?
Monosaccharides
What is the formula for a hexose sugar?
C6H12O6
C=O
Carbonyl
-OH
Hydroxyl
What two things do all sugars have?
Two functional groups (carbonyl and hydroxyl)
What is the difference between an aldehyde sugar and a ketone sugar?
The location of the carbonyl group is different.
What is the term for compounds that have the same molecular formulas but different structural formulas?
Isomers
Where are all the carbons in the ring structure?
Each unlabeled corner represents a carbon.
Maltose
Disaccharide — Glucose + Glucose
Sucrose
Disaccharide — Glucose + Fructose
Lactose
Disaccharide — Glucose + Galactose
What is a glycosidic linkage?
A covalent bond formed between two monosaccharides by dehydration synthesis.
What is a 1-4 glycosidic linkage?
The 1-carbon of a monosaccharide is joined to the 4-carbon on another monosaccharide.
What are the two types of polysaccharides? Give examples
Storage: Starch, Glycogen….Structural: Cellulose
Why can you not digest cellulose? What organisms can?
Enzymes are unable to hydrolyze the beta linkages due to its different shape. Some microorganisms can.
Has 1-4 Beta linkages
Cellulose
Is a storage polysaccharide produced by vertebrates, stored in your liver.
Glycogen
Two monomers of this form maltose.
Glucose
Glucose + Fructose = ?
Sucrose
Monosaccharide commonly called “fruit sugar”
Fructose
“Milk sugar”
Lactose
Structural polysaccharide that gives cockroaches their crunch
Chitin
Malt sugar; used to brew beer
Maltose
Structural polysaccharide that comprises plant cell walls
Cellulose
What characteristic do all lipids share?
Hydrophobia
What are the building blocks of fats?
Glycerol and fatty acids
If a fat is composed of 3 fatty acids and 1 glycerol molecule, how many water molecules will be removed to form it? What is this process called?
3–dehydration reaction
What does unsaturated mean?
A carbon is double bonded to another carbon and therefore the fatty acid has fewer hydrogens.
Name two saturated fats.
Lard, Butter
Name two unsaturated fats.
Olive Oil, Vegetable Oil
Why are many unsaturated fats liquid at room temperature?
The kinks where cis-double bonds are located prevent the molecules from packing tightly together.
List four important functions of fats.
Energy storage, heat, cushions vital organs, more efficient energy.
Why is the “tail” hydrophobic?
Hydrocarbons
What are other examples of steroids?
Sex hormones
Structural Protein
Function: Support, Ex.: Collagen
Storage Protein
Function: Amino Acid Storage, Ex.: Casein
Transport Protein
Function: Transportation, Ex.: Hemoglobin
Contractile Protein
Function: Movement, Ex. Actin
Enzymatic
Function: Acceleration of reactions, Ex.: Digestive enzymes
What is represented by an R-group? How many are there?
Side chains; there are 20.
Define dipeptide
A peptide of two amino acids and residues
Define polypeptide
Polymers of amino acids
Define Peptide bond
Covalent bond between two amino acids
Primary Protein Structure
Unique sequence of amino acids. Determined by DNA. Transthyretin is an example.
Secondary Protein Structure
Polypeptide chains repeatedly coiled that contribute to the protein’s overall shape. Alpha helix is an example.
Tertiary Protein Structure
Overall shape of a polypeptide. Hydrophobic interaction is an example.
Quaternary Protein Structure
Overall protein structure resulting from the oxygenation of the polypeptide. Collagen is an example.
Explain sickle-cell disease.
Caused by the substitution of one amino acid for the normal one. This changes the three-dimensional shape.
Define denaturation, and give three ways a protein may become denaturated.
The changing of a protein during which the protein loses its native shape because weak bonds have been destroyed. Alteration of pH, salt concentration, temperature.
Explain the flow of genetic information.
mRNA molecule interacts with the cell’s protein-synthesizing machinery to direct production of polypeptide, which folds into all or part of a protein. The sites of protein synthesis are tiny structures called ribosomes. Messenger RNA conveys genetic instructions for building proteins from nucleus to cytoplasm.
What are the components of a nucleic acid?
Sugar, nitrogenous base, phosphate group
Which four nitrogen bases are found in DNA?
Adenine, Thymine, Cytosine, Guanine
Which four are found in RNA?
Adenine, guanine, cytosine, uracil
How do ribose and deoxyribose sugars differ?
Deoxyribose sugar lacks an oxygen atom on the second carbon in the ring.
What is the shape of DNA called?
Double helix
Why are the strands of DNA said to be antiparallel?
They run in opposite 5′-3′ directions from each other.
What two molecules make up the “uprights”?
Sugar and phosphate
What molecules make up the rungs?
Base pairs joined by hydrogen bonds
How are the bases paired?
A-T, C-G