100 Biochemistry Flashcard Questions & Answers
Q: What is the simplest unit of a protein?
A: Amino acid.
Q: What type of bond links amino acids together in proteins?
A: Peptide bond.
Q: Which amino acid is classified as an imino acid?
A: Proline.
Q: What amino acid acts as an inhibitory neurotransmitter?
A: Glycine.
Q: Which sulfur-containing amino acids are common?
A: Methionine and Cysteine.
Q: What amino acids have non-polar alkyl R-groups?
A: Alanine, Valine, Leucine, Isoleucine, Proline.
Q: Name two aromatic amino acids.
A: Phenylalanine, Tryptophan.
Q: What is the structure of a primary protein?
A: Linear sequence of amino acids.
Q: What stabilizes secondary protein structures?
A: Hydrogen bonds.
Q: Name a protein with a beta-sheet structure.
A: Collagen or Keratin.
Q: What disease is caused by prion-induced beta-sheet misfolding?
A: Creutzfeldt-Jakob disease.
Q: What are the bonds in tertiary structure?
A: Disulfide, hydrogen, ionic, van der Waals.
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100 Biochemistry Flashcard Questions & Answers
Q: What are proteins assisting in folding called?
A: Chaperones.
Q: Give an example of a quaternary protein.
A: Hemoglobin.
Q: What causes protein denaturation?
A: Heat, urea.
Q: What is renaturation?
A: Recovery of native protein structure.
Q: What is the structural defect in Sickle Cell Anemia?
A: Glutamate -> Valine in beta-chain of hemoglobin.
Q: What is the main collagen type in bones?
A: Type I.
Q: What disease is caused by a defect in type I collagen?
A: Osteogenesis imperfecta.
Q: Which hormone is derived from proinsulin?
A: Insulin.
Q: What color indicates a positive Biuret test?
A: Violet.
Q: What does the Ninhydrin test detect?
A: Free amino groups.
Q: What does a yellow Xanthoproteic test result mean?
A: Presence of tyrosine/tryptophan.
Q: Which test is specific for tyrosine using mercury nitrate?
A: Millon's test.
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100 Biochemistry Flashcard Questions & Answers
Q: What test uses glyoxylic acid to detect tryptophan?
A: Hopkin's-Cole test.
Q: Which test turns red in the presence of cysteine?
A: Nitroprusside test.
Q: What test detects arginine?
A: Sakaguchi test.
Q: What are enzymes made of?
A: Proteins.
Q: What do enzymes do to activation energy?
A: Lower it.
Q: What happens to enzyme function above 37°C?
A: Degrades.
Q: What is a coenzyme?
A: A vitamin or ion helping enzyme action.
Q: What is the function of oxidoreductase?
A: Catalyzes redox reactions.
Q: What does transferase do?
A: Transfers functional groups.
Q: What enzyme type cleaves with water?
A: Hydrolase.
Q: What enzyme rearranges molecules?
A: Isomerase.
Q: What is competitive inhibition?
A: Inhibitor blocks active site.
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100 Biochemistry Flashcard Questions & Answers
Q: What is noncompetitive inhibition?
A: Inhibitor binds elsewhere, changes shape.
Q: What are isoenzymes?
A: Enzymes with different structure but same function.
Q: What are DNA's purines?
A: Adenine, Guanine.
Q: What are DNA's pyrimidines?
A: Cytosine, Thymine.
Q: What bonds link nucleotides?
A: Phosphodiester bonds.
Q: Who proposed DNA's double helix?
A: Watson and Crick.
Q: What bonds hold A-T together?
A: 2 hydrogen bonds.
Q: What is DNA denaturation?
A: Strand separation.
Q: What is DNA renaturation?
A: Reannealing of strands.
Q: What does RNA use instead of thymine?
A: Uracil.
Q: Which RNA forms ribosomes?
A: rRNA.
Q: What is the ribosome size in eukaryotes?
A: 80S (60S + 40S).
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100 Biochemistry Flashcard Questions & Answers
Q: What enzyme replicates DNA?
A: DNA polymerase.
Q: What is the function of helicase?
A: Unwinds DNA.
Q: What is the function of ligase?
A: Seals DNA fragments.
Q: What are Okazaki fragments?
A: Short DNA pieces on lagging strand.
Q: What is transcription?
A: DNA -> RNA synthesis.
Q: What is the TATA box in eukaryotes?
A: Hogness box.
Q: What inhibits RNA polymerase II?
A: alpha-Amanitin.
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