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CHM 130 Final Study Guide Questions And Answers Pass Guaranteed

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The function of the enzyme-substrate complex is to provide an alternative reaction pathway that ________. A) lowers the energy of the products B) lowers the energy of the substrate C) changes the concentration of the substrate D) lowers the activation energy for the reaction E) changes the possible product formed - correct answers lowers the activation energy for the reaction In the induced-fit model of enzyme action, the enzyme active site ________. A) stays the same shape during substrate binding B) adjusts shape to adapt to the shape of the substrate C) stays the same shape while causing a change in the shape of the substrate D) uses an inhibitor to adjust its shape for the substrate E) uses a cofactor to change the shape of a substrate - correct answers adjusts shape to adapt to the shape of the substrate A noncompetitive inhibitor ________. A) binds at the active site of the enzyme B) alters the three-dimensional structure of the enzyme C) increases the rate of the enzyme-catalyzed reaction D) has a structure similar to the substrate E) has its effect reversed by adding more substrate - correct answers alters the three-dimensional structure of the enzyme Which of the following is not true for a competitive inhibitor? A) It occupies the active site. B) It cannot be converted to products. C) It has a structure similar to the substrate. D) Increasing the substrate concentration can reverse competitive inhibition. E) It binds to the enzyme at a site remote from the active site. - correct answers It binds to the enzyme at a site remote from the active site. The formation of an enzyme-substrate complex is the ________ step in enzyme action. A) first B) second C) third D) fourth E) last - correct answers first 309. The presence of enzymes to catalyze bioreactions in our bodies allows ________. A) us to eat non-nutritious substances without consequence B) the activation energy of a reaction to be raised C) the rate of a desired chemical reaction to slow down D) bioreactions to occur under extreme conditions of temperature and pH E) bioreactions to take place under mild conditions - correct answers bioreactions to take place under mild conditions 308. The names of many enzymes can be recognized by the suffix ________. A) ate B) ite C) ose D) ine E) ase - correct answers ase 307. The general function of an enzyme in the body is to ________. A) catalyze chemical reactions B) maintain a neutral pH C) act as a reactant in carbohydrate storage D) maintain homeostasis E) eliminate waste products from the blood - correct answers catalyze chemical reactions 305. Heavy metals denature proteins by ________. A) releasing amino acids B) disrupting hydrophobic interactions C) changing the pH of the protein solution D) changing the temperature of the protein solution E) disrupting disulfide bonds - correct answers disrupting disulfide bonds 304. The structure of collagen consists of ________. A) single α-helix strands B) double α-helix strands C) many α-helixes wound into fibrils D) a braided triple helix E) many glycoside links - correct answers a braided triple helix 303. What kinds of interactions are not part of tertiary protein structure? A) peptide bonds B) disulfide bonds C) hydrophilic interactions D) salt bridges E) hydrophobic interactions - correct answers peptide bonds 302. Which of the following is a secondary protein structure? A) α-helix B) Ser-Met-Ala-Gly-Ile C) disulfide bond D) salt bridges E) hydrophobic interactions - correct answers α-helix 301. The attractive forces that are important in the secondary structure of a protein are ________. A) hydrogen bonds B) hydrophobic interactions C) disulfide bonds D) salt bridges E) peptide bonds - correct answers hydrogen bonds 300. In insulin, two peptide chains are held together in a single unit by ________. A) disulfide bridges B) hydrogen bonds C) salt bridges D) a prosthetic group E) a β-pleated sheet - correct answers disulfide bridges 299. In the peptide Ala-Try-Gly-Phe, the C-terminus is ________. A) alanine B) phenylalanine C) tryptophan D) aspartate E) glycine - correct answers phenylalanine 298. In the peptide Ala-Try-Gly-Phe, the N-terminus is ________. A) alanine B) phenylalanine C) tryptophan D) aspartate E) glycine - correct answers alanine 297. The peptide bonds that link amino acids in a protein are ________. A) ester bonds B) ether bonds C) amide bonds D) glycosidic bonds E) sulfide bonds - correct answers amide bonds 295. The side chain for valine is classified as a ________ side chain. A) basic B) neutral C) acidic D) nonpolar E) polar - correct answers nonpolar 294. The side chain for histidine is classified as a ________ side chain. A) basic B) neutral C) acidic D) nonpolar E) polar - correct answers basic 293. The structural formulas of amino acids are the same except for the ________. A) carboxylate group B) alpha carbon C) ammonium group D) R group E) hydrogen bonding - correct answers R group 292. In the ionized form of an amino acid, the carboxylic acid end is ________. A) positively charged B) negatively charged C) neutral D) soluble in a nonpolar solvent E) attached to an amine - correct answers negatively charged 291. Sucrase, the protein that facilitates the hydrolysis of sucrose, would be classified as a __

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Instelling
CHM 130
Vak
CHM 130

Voorbeeld van de inhoud

CHM 130 Final Study Guide Questions
And Answers Pass Guaranteed

The function of the enzyme-substrate complex is to provide an alternative reaction pathway that
________.



A) lowers the energy of the products

B) lowers the energy of the substrate

C) changes the concentration of the substrate

D) lowers the activation energy for the reaction

E) changes the possible product formed - correct answers lowers the activation energy for the reaction



In the induced-fit model of enzyme action, the enzyme active site ________.



A) stays the same shape during substrate binding

B) adjusts shape to adapt to the shape of the substrate

C) stays the same shape while causing a change in the shape of the substrate

D) uses an inhibitor to adjust its shape for the substrate

E) uses a cofactor to change the shape of a substrate - correct answers adjusts shape to adapt to the
shape of the substrate



A noncompetitive inhibitor ________.



A) binds at the active site of the enzyme

B) alters the three-dimensional structure of the enzyme

C) increases the rate of the enzyme-catalyzed reaction

D) has a structure similar to the substrate

,E) has its effect reversed by adding more substrate - correct answers alters the three-dimensional
structure of the enzyme



Which of the following is not true for a competitive inhibitor?



A) It occupies the active site.

B) It cannot be converted to products.

C) It has a structure similar to the substrate.

D) Increasing the substrate concentration can reverse competitive inhibition.

E) It binds to the enzyme at a site remote from the active site. - correct answers It binds to the enzyme
at a site remote from the active site.



The formation of an enzyme-substrate complex is the ________ step in enzyme action.



A) first

B) second

C) third

D) fourth

E) last - correct answers first



309. The presence of enzymes to catalyze bioreactions in our bodies allows ________.



A) us to eat non-nutritious substances without consequence

B) the activation energy of a reaction to be raised

C) the rate of a desired chemical reaction to slow down

D) bioreactions to occur under extreme conditions of temperature and pH

E) bioreactions to take place under mild conditions - correct answers bioreactions to take place under
mild conditions



308. The names of many enzymes can be recognized by the suffix ________.

,A) ate

B) ite

C) ose

D) ine

E) ase - correct answers ase



307. The general function of an enzyme in the body is to ________.



A) catalyze chemical reactions

B) maintain a neutral pH

C) act as a reactant in carbohydrate storage

D) maintain homeostasis

E) eliminate waste products from the blood - correct answers catalyze chemical reactions



305. Heavy metals denature proteins by ________.



A) releasing amino acids

B) disrupting hydrophobic interactions

C) changing the pH of the protein solution

D) changing the temperature of the protein solution

E) disrupting disulfide bonds - correct answers disrupting disulfide bonds



304. The structure of collagen consists of ________.



A) single α-helix strands

B) double α-helix strands

C) many α-helixes wound into fibrils

D) a braided triple helix

, E) many glycoside links - correct answers a braided triple helix



303. What kinds of interactions are not part of tertiary protein structure?



A) peptide bonds

B) disulfide bonds

C) hydrophilic interactions

D) salt bridges

E) hydrophobic interactions - correct answers peptide bonds



302. Which of the following is a secondary protein structure?



A) α-helix

B) Ser-Met-Ala-Gly-Ile

C) disulfide bond

D) salt bridges

E) hydrophobic interactions - correct answers α-helix



301. The attractive forces that are important in the secondary structure of a protein are ________.



A) hydrogen bonds

B) hydrophobic interactions

C) disulfide bonds

D) salt bridges

E) peptide bonds - correct answers hydrogen bonds



300. In insulin, two peptide chains are held together in a single unit by ________.



A) disulfide bridges

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CHM 130

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