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Protein structure— formative assessment AP Biology 10/7/2013
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Level 2.0
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1. What is the name for the variable region of the 20 amino acids? 1.Carboxyl group 2.Amino group 3.R group 4.Alpha Carbon
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2. What functional group must be present in the R group of an acidic (-) amino acid? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.Sulfahydryl group
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3. What functional group must be present in the R group of a basic (+) amino acid? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.Sulfahydryl group
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4. What functional group is most often present in a neutral, yet hydrophilic, amino acid’s R group? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.phosphate group 5.sulfahydryl
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5. What functional group in cysteine and methionine allows them to form strong covalent bonds that stabilize a protein’s tertiary structure? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.Sulfahydryl group
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6. Which arrow points to a peptide bond? 1.a 2.b 3.c 4.d a ab c d
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Level 3.0
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7. How do alpha helices and Beta pleated sheets compare? 1.They are both forms of protein secondary structure 2.They are both formed due to formation of H bonds between N-H & C=O groups along the backbone of polypeptide chain 3.The beta sheets are more rigid & strong because they form more abundant H bonds 4.All of the above
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8. R group interactions control which levels of protein folding? 1.Primary structure & secondary structure 2.Secondary structure only 3.Tertiary & quartenary structure 4.Tertiary structure only 5.Quartenary structure only
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9. Which amino acids tend to cluster in the center of an aqueous protein, but to be located on the outer edges of proteins located within a cell membrane’s lipid bilayer? 1.Acidic amino acids 2.Basic amino acids 3.Disulfide bridge forming cysteines & methionines 4.Polar, hydrophilic amino acids 5.Nonpolar, hydrophobic amino acids
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10 Primary protein structure A.Is directly defined by the genetic code B.Is the linear order of amino acids C.Includes peptide bonds of the backbone D.All of the above
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11. Secondary structure is due to: A.Peptide bonding B.R group acidic & basic interaction C.H bonding between carbonyl & amino groups of backbone D.H bonding between carboxyl & amino groups in R groups of different amino acids
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12. Which interactions are most important in making denatured proteins clump together? A.Acid/base R group interaction B.Hydrophobic R group interactions C.Hydrophilic R group interactions D.Disulfide bridges
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13. Write the order of strength of these interactions in determining tertiary structure? A.Vanderwaals forces of hydrophobic R group interactions B.Hydrogen bonding of hydrophilic, yet neutral R group interactions C.Acidic & Basic R group interactions D.Disulfide bridges of methionine to methionine or cysteine to cysteine
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14. Give an example of a quarternary structure. Enter Answer Text
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If your answers were correct for 8 or 9 questions, then you should work independently on Stanford notes for Chapter 6. This power point will be online for your use in studying. If you answered 7 or fewer questions correctly, you should review the next explanation slides.
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1. What is the name for the variable region of the 20 amino acids? 1.Carboxyl group 2.Amino group 3.R group 4.Alpha Carbon
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Every amino acid contains a central (α) C, surrounded by a H, an R group (variable group), an amino group, and a carboxyl group. The amino group acts as a base, accepting a protons, whereas the carboxyl group acts as an acid, donating a proton.
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2. What functional group must be present in the R group of an acidic (-) amino acid? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.Sulfahydryl group
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About 1 x 10 -7 Moles water /L dissociates to produce H + ions and OH - ions. The ratio of the two ions is 1.0, and the pH is 7—neutral. When substances known as acids are dissolved in water, then they dissociate to produce H + ions, making the H + :OH - ratio higher than 1.0. Acids are proton donors when dissolved in aqueous solution. Carboxyl groups behave as acids because they dissociate to release H + ions. The amino acids aspartic acid & glutamic acids have a carboxyl group in their group, so they are acidic amino acids.
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3. What functional group must be present in the R group of a basic (+) amino acid? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.Sulfahydryl group
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Bases either release OH - OR accept H + ions when dissolved in aqueous solution. In both cases, bases reduce the H + : OH - ratio to less than 1.0 The amino group in an amino acid’s R group acts as a base, accepting a proton. The amino acids arginine and lysine act as bases.
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4. What functional group is most often present in a neutral, yet hydrophilic, amino acid’s R group? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.sulfahydryl
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5. What functional group in cysteine and methionine allows them to form strong covalent bonds that stabilize a protein’s tertiary structure? 1.Carboxyl group 2.Amino group 3.Hydroxyl group 4.Carbonyl group 5.Sulfahydryl group
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6. Which arrow points to a peptide bond? 1.a 2.b 3.c 4.d a ab c d
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Level 3.0
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7. How do alpha helices and Beta pleated sheets compare? 1.They are both forms of protein secondary structure 2.They are both formed due to formation of H bonds between N-H & C=O groups along the backbone of polypeptide chain 3.The beta sheets are more rigid & strong because they form more abundant H bonds 4.All of the above
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Protein structure
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8. R group interactions control which levels of protein folding? 1.Primary structure & secondary structure 2.Secondary structure only 3.Tertiary & quartenary structure 4.Tertiary structure only 5.Quartenary structure only
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R group interactions control tertiary & Quarternary structure
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9. Which amino acids tend to cluster in the center of an aqueous protein, but to be located on the outer edges of proteins located within a cell membrane’s lipid bilayer? 1.Acidic amino acids 2.Basic amino acids 3.Disulfide bridge forming cysteines & methionines 4.Polar, hydrophilic amino acids 5.Nonpolar, hydrophobic amino acids
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