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Test Bank - Lehninger Principles of Biochemistry, 7th Edition (Nelson, 2018) Chapter 1-28 | All Chapters
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aqueous environment? A. Ionic interactions B. Hydrogen bonds C. Van der Waals interactions
The hydrophobic effect drives nonpolar side chains into the interior of proteins, minimizing contact with water and stabilizing the folded structure.
A. The overall 3D shape
C. Alpha-helices and beta-sheets D. Multiple polypeptide chains interacting The primary structure is the linear sequence of amino acids in a polypeptide chain.
A. Maximum velocity
B. Catalytic efficiency
D. Turnover number Km reflects the substrate concentration at which the reaction rate is half of Vmax, indicating enzyme affinity for substrate.
A. Alanine
C. Serine D. Lysine Cysteine has a thiol (-SH) group, which can form disulfide bonds important for protein structure.
A. Cytosine B. Thymine
D. Uracil Purines have a two-ring structure; guanine and adenine are purines.
A. Covalent bonds between bases B. Phosphodiester bonds between base pairs
D. Glycosidic linkages
A. Enzyme activator
C. Proton pump D. Structural protein NAD+ accepts electrons during redox reactions, becoming NADH, and serves as an electron carrier.
A. Complex I B. Complex III
D. Complex IV Complex II (succinate dehydrogenase) transfers electrons but does not contribute to the proton gradient.
A. PEP carboxylase
C. Malate dehydrogenase D. Pyruvate carboxylase Rubisco catalyzes the fixation of CO₂ to ribulose-1,5-bisphosphate in the Calvin cycle.
A. Brain B. Muscle
D. Pancreas The liver is the primary organ responsible for producing glucose from non- carbohydrate sources.
A. Vitamin B
C. Vitamin B D. Vitamin B Pantothenic acid is a precursor to coenzyme A, essential in metabolism.
A. An active enzyme
C. A substrate analog D. A cofactor Zymogens are inactive forms of enzymes that require cleavage for activation (e.g., trypsinogen).
A. Triacylglycerol
A. Unwinds DNA
C. Synthesizes RNA primers D. Synthesizes new DNA strands DNA ligase forms phosphodiester bonds to seal breaks in the DNA backbone.
A. Hydrophobic only B. Hydrophilic only
D. Non-polar Amphipathic molecules like phospholipids contain both polar and non-polar regions.
A. Glycolysis
C. Fermentation D. Gluconeogenesis The electron transport chain uses oxygen as the final electron acceptor.
A. Degrade misfolded proteins B. Catalyze chemical reactions
D. Cleave signal peptides Molecular chaperones assist proteins in reaching their correct conformation.
A. Glycolysis B. TCA cycle
D. Gluconeogenesis Oxidative phosphorylation, driven by the proton gradient, yields the most ATP.
A. Ionic bonds B. Disulfide bridges
D. Van der Waals interactions Hydrogen bonding between the carbonyl and amide groups stabilizes alpha- helices.
A. Pyruvate kinase
C. Phosphofructokinase D. Aldolase
C. kcat D. Turnover number Competitive inhibitors increase Km but do not affect Vmax.
A. Pyruvate B. Glucose
D. Succinyl-CoA Acetyl-CoA condenses with oxaloacetate to form citrate, starting the TCA cycle.
A. Hydrolases B. Transferases
D. Isomerases Oxidoreductases facilitate electron transfer in redox reactions.
A. Deoxyribose
C. Fructose D. Galactose RNA contains ribose, which has a hydroxyl group at the 2’ carbon.
A. Peptide bond
C. Hydrogen bond D. Phosphodiester bond Glycosidic bonds form between hydroxyl groups of monosaccharides.
A. Protein → RNA → DNA B. DNA → Protein → RNA
D. RNA → DNA → Protein The central dogma states that genetic information flows from DNA to RNA to protein.
A. Helicase
C. Primase D. Ligase Topoisomerases cut and rejoin DNA strands to relieve torsional stress.
A. Glycolysis
C. Beta-oxidation
A. Competitive B. Noncompetitive
D. Allosteric Uncompetitive inhibitors bind exclusively to the enzyme-substrate complex, lowering both Km and Vmax.
A. Serine B. Glutamate
D. Asparagine Leucine is purely ketogenic, contributing only to acetyl-CoA or ketone bodies.
chain? A. A site
C. E site D. T site The P site (peptidyl site) holds the tRNA with the growing peptide chain.
D. Coenzyme Q SAM is a common methyl donor in methylation reactions.
Oxygen accepts electrons at the end of the chain, forming water.
A. DNA polymerase B. Ligase
D. Helicase Primase lays down short RNA primers to initiate DNA synthesis.
A. Phosphatidylcholine B. Sphingomyelin
D. Triacylglycerol Cholesterol serves as the biosynthetic precursor for all steroid hormones.
A. Binding at the active site
D. Coenzyme A PLP (derived from vitamin B6) is essential for transferring amino groups.
A. Thymine
C. Guanine D. Cytosine In RNA, uracil replaces thymine and pairs with adenine.
D. Glucose The Calvin cycle incorporates CO₂ into organic molecules through carbon fixation.
A. ATP synthase
C. Citrate synthase D. Succinate dehydrogenase PDC converts pyruvate into acetyl-CoA, linking glycolysis to the TCA cycle.
A. Uracil
C. Cytosine D. Adenine Thymine is found only in DNA; uracil replaces it in RNA.
A. Random and overlapping B. Each codon codes for multiple amino acids
D. Redundant and ambiguous The code is degenerate (multiple codons per amino acid) but each codon is read independently (non-overlapping).
A. Addition of NH₄⁺
C. Addition of phosphate D. Oxidation of fatty acids Oxidative deamination removes an amino group from an amino acid, releasing ammonia.
A. Alanine
C. Tyrosine D. Glutamine Lysine cannot be synthesized by humans and must be obtained from the diet.
A. ATP → ADP + Pi
ATP synthase synthesizes ATP from ADP and inorganic phosphate using the proton gradient.
A. Activates glycolysis B. Carries amino acids
D. Generates NADPH Carnitine shuttles long-chain fatty acids across the mitochondrial membrane for β- oxidation.
A. Acetyl-CoA B. Ethanol
D. Oxaloacetate In anaerobic muscle, pyruvate is reduced to lactate to regenerate NAD⁺ for glycolysis.
A. Riboflavin
B. Biotin
D. Thiamine Niacin (vitamin B3) is the precursor for NAD⁺, a key redox cofactor.
A. Redox
C. Hydrolysis D. Isomerization Kinases transfer phosphate groups from ATP to substrates.
respiration? A. ATP donor B. Reducing agent
D. Coenzyme Oxygen accepts electrons at the end of the electron transport chain to form water.
A. Biotin
D. CoA