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AP Bio Exam: Unit 1
Review for Unit 1
| Term | Definition |
|---|---|
| What is a polar covalent bond? | A covalent bond where electrons are shared unequally between atoms, resulting in partial charges. |
| Where is the polar covalent bond in a water molecule? | Between the oxygen and hydrogen atoms. |
| Diagram a water molecule including the polar bond and partial charges labeled. | A diagram showing oxygen with partial negative charge and hydrogens with partial positive charges, with polar covalent bonds between them. |
| Describe why water is considered a polar molecule. | Water has a bent shape with unequal electron sharing, creating partial positive and negative ends. |
| What is a hydrogen bond? | A weak attraction between a hydrogen atom in a polar molecule and an electronegative atom in another molecule. |
| Where are hydrogen bonds found in water? | Between the hydrogen of one water molecule and the oxygen of another. |
| Draw a diagram of TWO molecules including the hydrogen bond and polar bonds labeled. | A diagram showing two water molecules with polar covalent bonds within each and hydrogen bonds between them. |
| Identify three properties of water. | Cohesion, adhesion, and high specific heat capacity. |
| What is specific heat capacity? | The amount of heat required to raise the temperature of a substance by one degree Celsius. |
| Describe how water has a high specific heat capacity. | Water forms many hydrogen bonds, requiring significant energy to break them and increase temperature. |
| What is evaporative cooling? | The cooling effect caused by the evaporation of water from a surface. |
| Describe how water is able to facilitate evaporative cooling. | Water molecules with high kinetic energy evaporate, removing heat and lowering the temperature of the remaining liquid. |
| Describe two ways that organisms maintain body temperatures. | Sweating and panting. |
| Describe a hydrogen bond. | A weak attraction between a hydrogen atom in a polar molecule and an electronegative atom in another molecule. |
| Identify THREE properties of water that are caused by hydrogen bonding. | Cohesion, adhesion, and high surface tension. |
| Compare and contrast cohesion and adhesion. | Cohesion is water sticking to water; adhesion is water sticking to other surfaces. |
| What is surface tension? | The measure of how difficult it is to stretch or break the surface of a liquid. |
| Which of the properties of water causes surface tension? | Cohesion. |
| Using the properties of water, describe how water can move up a capillary tube to move from the roots to the leaves in a plant. | Adhesion to the tube walls and cohesion between water molecules create a continuous column. |
| Using the properties of water, describe how a water strider can walk on water. | Surface tension, caused by cohesive hydrogen bonds, supports the strider’s weight. |
| What are the four macromolecules? | Carbohydrates, lipids, proteins, and nucleic acids. |
| What are the elements found in a carbohydrate? | Carbon, hydrogen, and oxygen. |
| What are three functions of carbohydrates in living organisms? | Energy storage, structural support, and cell recognition. |
| What are the elements found in a protein? | Carbon, hydrogen, oxygen, nitrogen, and sulfur. |
| What are the functional groups found in all amino acids? | Amino group and carboxyl group. |
| What are three functions of proteins in living organisms? | Enzymes, structural support, and transport. |
| What are the elements found in a lipid? | Carbon, hydrogen, and oxygen. |
| How are the three different types of lipids different? | Fats store energy, phospholipids form membranes, and steroids act as hormones. |
| What are three functions of lipids in living organisms? | Energy storage, insulation, and cell membrane formation. |
| What are the elements found in nucleic acids? | Carbon, hydrogen, oxygen, nitrogen, and phosphorus. |
| What are parts found in all nucleotides? | A phosphate group, a five‑carbon sugar, and a nitrogenous base. |
| What are three functions of nucleic acids in living organisms? | Storing genetic information, transmitting genetic information, and catalyzing reactions. |
| Which macromolecule(s) contain sulfur? | Proteins. |
| Which macromolecule(s) contain phosphorus? | Nucleic acids and phospholipids. |
| Which macromolecule(s) contain nitrogen? | Proteins and nucleic acids. |
| What is a hydrolysis reaction? | A reaction that breaks bonds by adding water. |
| Describe the process of a hydrolysis reaction. | Water molecules split, breaking bonds between monomers and adding hydroxyl and hydrogen groups. |
| Identify inputs and outputs of a hydrolysis reaction using a specific example. | Input: Disaccharide + Water; Output: Two Monosaccharides. |
| What type of bond is found in carbohydrate monomers? | Glycosidic linkage. |
| Specifically, where is this bond located? | Between the hydroxyl groups of two monosaccharides. |
| What type of bond is found between protein monomers? | Peptide bond. |
| Specifically, where is this bond located? | Between the carboxyl group of one amino acid and the amino group of another. |
| What type of bond is found between nucleic acid monomers? | Phosphodiester bond. |
| Specifically, where is this bond located? | Between the phosphate group of one nucleotide and the sugar of another. |
| What is a dehydration synthesis reaction? | A reaction that forms bonds by removing water. |
| Describe the process of a dehydration synthesis reaction. | Monomers join, releasing a water molecule formed from hydroxyl and hydrogen groups. |
| Identify inputs and outputs of a dehydration synthesis reaction using a specific example. | Input: Two Monosaccharides; Output: Disaccharide + Water. |
| Diagram a dehydration synthesis reaction of two carbohydrate monomers including a label on the bond. | A diagram showing two monosaccharides joining with a water molecule removed and a glycosidic bond formed. |
| Diagram a dehydration synthesis reaction of two protein monomers including a label on the bond. | A diagram showing two amino acids joining with a water molecule removed and a peptide bond formed. |
| Diagram a dehydration synthesis reaction of two nucleic acid monomers including a label on the bond. | A diagram showing two nucleotides joining with a water molecule removed and a phosphodiester bond formed. |
| Diagram a dehydration synthesis reaction of glycerol and fatty acids. | A diagram showing glycerol and fatty acids joining with water molecules removed to form ester bonds. |
| What is the monomer of a carbohydrate? | Monosaccharide. |
| Identify the components of the monomer. | Carbon, hydrogen, and oxygen in a 1:2:1 ratio. |
| Diagram a carbohydrate monomer labeling the components. | A diagram showing a hexagonal ring with carbon, hydrogen, and oxygen atoms labeled. |
| Diagram a disaccharide labeling the bond between the monomers. | A diagram showing two monosaccharides connected by a glycosidic linkage. |
| What type of bond is found between carbohydrate monomers? | Glycosidic linkage. |
| Describe the structures of a monosaccharide and a polysaccharide. | Monosaccharides are single sugar units; polysaccharides are long chains of monosaccharides. |
| Describe the structures of starch and cellulose. | Starch is a helical chain of glucose; cellulose is a straight chain with hydrogen bonds. |
| What type of bond is found in starch? | Alpha glycosidic linkage. |
| What type of bond is found in cellulose? | Beta glycosidic linkage. |
| Which bond can be broken by animals? | Alpha glycosidic linkage. |
| Describe two functions of carbohydrates. | Energy storage and structural support. |
| Identify the property of lipids. | They are hydrophobic and nonpolar. |
| How is this different than the other macromolecules? | Other macromolecules are generally polar or hydrophilic. |
| Describe the structure of a saturated fatty acid. | Straight chain with no double bonds between carbon atoms. |
| Describe the structure of an unsaturated fatty acid. | Kinked chain with one or more double bonds between carbon atoms. |
| How does the level of saturation affect the fatty acid at room temperature? | Saturated fats are solid; unsaturated fats are liquid. |
| What would happen if the level of saturation was increased? | The fatty acid would become more solid at room temperature. |
| What would happen if the level of saturation was decreased? | The fatty acid would become more liquid at room temperature. |
| Identify the three main types of lipid macromolecules. | Fats, phospholipids, and steroids. |
| Describe the structure of a fat molecule. | Three fatty acids attached to a glycerol backbone via ester bonds. |
| Identify the function of fats. | Long‑term energy storage. |
| Describe the general structure of steroids. | Four fused carbon rings. |
| How does the structure of cholesterol compare? | Cholesterol is a steroid with a hydroxyl group and a hydrocarbon tail. |
| Describe the function of steroids. | Acting as hormones and signaling molecules. |
| Describe the function of cholesterol. | Maintaining membrane fluidity and serving as a precursor for steroids. |
| Diagram and label the structure of a phospholipid. | A diagram showing a glycerol, two fatty acids, a phosphate group, and a polar head. |
| Identify the function of phospholipids. | Forming the lipid bilayer of cell membranes. |
| How does the structure of saturated and unsaturated fatty acids differ? | Saturated fats are straight; unsaturated fats have kinks due to double bonds. |
| How does the level of saturation affect the function of the lipid? | Saturated fats increase membrane rigidity; unsaturated fats increase fluidity. |
| What is the monomer of a nucleic acid? | Nucleotide. |
| Diagram the monomer of a nucleic acid and label the structural components. | A diagram showing a phosphate group, a five‑carbon sugar, and a nitrogenous base. |
| Identify the FIVE nitrogenous bases. | Adenine, thymine, cytosine, guanine, and uracil. |
| Describe the difference between a purine and pyrimidine. | Purines have two rings; pyrimidines have one ring. |
| Identify which nitrogenous bases are purines. | Adenine and guanine. |
| Identify which nitrogenous bases are pyrimidines. | Thymine, cytosine, and uracil. |
| Describe the structure of the nucleic acid polymer. | A chain of nucleotides linked by phosphodiester bonds. |
| What are the ends called and what functional group is found at each end? | 5’ end has a phosphate; 3’ end has a hydroxyl group. |
| Describe the directionality of a nucleic acid. | Antiparallel, with one strand running 5’ to 3’ and the other 3’ to 5’. |
| Which end is the location of the growing nucleic acid strand? | The 3’ end. |
| Describe the structure of DNA. | Double helix with two strands of nucleotides held together by hydrogen bonds. |
| What are the complementary base pairings found in DNA? | Adenine with thymine; cytosine with guanine. |
| What are the complementary base pairings found in RNA? | Adenine with uracil; cytosine with guanine. |
| What type of bond occurs between complementary base pairings in DNA or RNA? | Hydrogen bond. |
| Describe or diagram where this bond is located. | Between nitrogenous bases on opposite strands. |
| What are the three components of a DNA or RNA monomer? | A phosphate group, a five‑carbon sugar, and a nitrogenous base. |
| Identify differences between DNA and RNA. | DNA has deoxyribose, thymine, and is double‑stranded; RNA has ribose, uracil, and is single‑stranded. |
| Describe the bonding between protein monomers including the functional group involved. | Peptide bonds form between the carboxyl group of one amino acid and the amino group of another. |
| Diagram the functional groups of carboxyl group and amino group. | A diagram showing a carboxyl group (COOH) and an amino group (NH2). |
| What are the ends of a protein called and what is found at each end? | N‑terminus has an amino group; C‑terminus has a carboxyl group. |
| Diagram the dehydration synthesis reaction of a growing polypeptide chain including a label for the location of the growing polypeptide strand. | A diagram showing amino acids joining at the C‑terminus with water removed. |
| What is the monomer of proteins? | Amino acid. |
| Identify the components of the monomer. | A central carbon, an amino group, a carboxyl group, a hydrogen, and an R group. |
| Describe how to determine the polarity of an R group. | Check if the R group is charged or polar. |
| Using the blue shaded R group, identify the group as hydrophobic, hydrophilic, or charged. | Hydrophobic if nonpolar; hydrophilic if polar; charged if ionic. |
| What is the primary structure of a protein? | The sequence of amino acids in a polypeptide chain. |
| What type of bond is involved with the primary structure of a protein? | Peptide bonds. |
| Diagram a primary structure of a protein labeling the components and bond. | A diagram showing a chain of amino acids connected by peptide bonds. |
| Describe the function of the primary structure. | Determines the protein’s overall structure and function. |
| How would an amino acid change affect the primary structure? | It would alter the sequence of amino acids. |
| What is the secondary structure of a protein? | Local folding into alpha helices or beta sheets stabilized by hydrogen bonds. |
| What type of bond is involved with the secondary structure of a protein? | Hydrogen bonds between the backbone atoms. |
| Describe the two structural shapes formed from bonding in the secondary structure. | Alpha helix and beta pleated sheet. |
| Diagram a secondary structure of a protein labeling the components, bond, and the structural shape. | A diagram showing a coiled alpha helix or folded beta sheet with hydrogen bonds. |
| Describe the function of the secondary structure. | Provides stability and contributes to the protein’s overall shape. |
| How would an amino acid change affect the secondary structure? | It could disrupt hydrogen bonding and alter folding. |
| What is the tertiary structure of a protein? | The overall 3D shape of a single polypeptide chain. |
| What type of bond(s) is/are involved with the tertiary structure of a protein? | Hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. |
| Diagram a tertiary structure of a protein labeling the components and bond(s). | A diagram showing a folded polypeptide with various interactions labeled. |
| Describe the function of the tertiary structure. | Determines the protein’s specific function and interaction sites. |
| How would an amino acid change affect the tertiary structure? | It could disrupt folding and alter function. |
| What is the quaternary structure of a protein? | The arrangement of multiple polypeptide chains into a functional protein complex. |
| What type of bond(s) is/are involved with the quaternary structure of a protein? | Same as tertiary: hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. |
| Diagram a quaternary structure of a protein labeling the components and bond(s). | A diagram showing multiple subunits interacting with various bonds. |
| Describe the function of the quaternary structure. | Enables complex functions like allosteric regulation and multi‑subunit activity. |
| How would an amino acid change affect the quaternary structure? | It could disrupt subunit interactions and overall function. |
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