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Which reaction is capable of breaking polypeptides into their component amino acids?


A) hydrogenation (adding hydrogen)
B) hydrolysis (adding water)
C) dehydrogenation (removing hydrogen)
D) dehydration (removing water)

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Alanine is the only α\alpha -amino acid that does not have a chiral carbon.

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Organic compounds that are not polypeptides but are necessary for enzymes to properly function are called ___.


A) substrates
B) zymogens
C) active sites
D) coenzymes

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Shown here is the amino acid glycine at a pH of ___. Shown here is the amino acid glycine at a pH of ___.   A)  1 B)  7 C)  14 D)  both 1 and 14


A) 1
B) 7
C) 14
D) both 1 and 14

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The peptide bond that connects amino acids in proteins is actually an ___ linkage.


A) amine
B) amide
C) ether
D) ester

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An enzyme displays ___ when the enzyme accepts only one specific substrate.


A) absolute specificity
B) relative specificity
C) stereospecificity
D) no specificity

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Enzymes that only catalyze the reaction of a particular stereoisomer are referred to as ___.

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Where is the peptide bond located in this dipeptide? Where is the peptide bond located in this dipeptide?   A)  the CO-NH joining serine and the valine B)  the doubly bonded oxygen just left of center between the amino acids C)  the CH-CO on the top of the serine going to the right D)  the NH-CH between the serine and valine


A) the CO-NH joining serine and the valine
B) the doubly bonded oxygen just left of center between the amino acids
C) the CH-CO on the top of the serine going to the right
D) the NH-CH between the serine and valine

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What form does isoleucine take at pH 14?


A) What form does isoleucine take at pH 14? A)    B)    C)    D)
B) What form does isoleucine take at pH 14? A)    B)    C)    D)
C) What form does isoleucine take at pH 14? A)    B)    C)    D)
D) What form does isoleucine take at pH 14? A)    B)    C)    D)

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Given the following amino acids and their R groups: glycine (R group is -H) - aspartic acid (R group is -CH2COO-) cysteine (R group is -CH2SH) - lysine (R group is -(CH2)4NH3+) Which amino acid is not optically active?

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Define the term zymogen. Explain why some enzymes are initially produced as zymogens.

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A zymogen is an enzyme precurs...

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A tetrapeptide is given as: Ser-Lys-Ala-Pro. Which of the following statements is true?


A) The serine provided a nitrogen for the peptide bond.
B) The N-terminus is serine (Ser) .
C) There are four peptide bonds because there are four amino acids.
D) The listing should be in alphabetical order.

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Catalysts, including enzymes, have the role of


A) changing a nonspontaneous chemical reaction to spontaneous.
B) lowering the activation energy of a reaction.
C) heating up the reactants to make the reaction progress faster.
D) changing the pH to a favorable pH for the reaction to progress.

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A change in pH usually produces a change in enzyme activity because


A) pH of the environment changes the conformation of the enzyme.
B) enzyme activity increases at extreme pH values (either acidic or basic) .
C) enzyme activity is usually least active below its optimum pH.
D) enzyme activity is most active above its optimum temperature.

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Classify each amino acid side chain as (nonpolar, polar-acidic, polar-neutral, or polar-basic.) a. glycine __________ b. aspartic acid __________ c. cysteine __________ c. lysine __________

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a. nonpolar
b. pola...

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As in α-helix, and the β-sheet are held together by ___ between amide-N-H and C=O groups.

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Which interactions are involved in establishing and holding the three-dimensional structure of a protein?


A) salt bridge and disulfide bonds
B) hydrogen bonds
C) hydrophobic effects
D) all of these choices

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If an amino acid is in a neutral solution, the form the carboxyl group takes is ___.


A) -CO2-
B) -CO2H+
C) -CO2-
D) -CO2H

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Leucine-enkephalin, a pentapeptide, is a naturally occurring pain reliever found in the brain. How many peptide bonds are there in leucine-enkephalin?


A) 5
B) 4
C) 6
D) 3

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Draw the dipeptide Asp-Ser and label the peptide bond, the N-terminus, and the C-terminus.

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