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CPC Biochemistry & Biological Chemistry Flashcards

6 cards from real CPC practice questions. Tap to flip, then mark Knew It or Still Learning — missed cards come back until you master them.

Read the first 6 CPC Biochemistry & Biological Chemistry flashcards as text

  1. Competitive inhibition of an enzyme is characterized by:

    Answer: Unchanged Vmax and increased apparent Km

    Competitive inhibitors bind at the active site, competing with substrate; high [S] can overcome inhibition, so Vmax is unchanged, but apparent Km increases (lower apparent affinity).

  2. Which reaction is catalyzed by DNA polymerase during DNA replication?

    Answer: Adding nucleotides to the 3'-OH end of a growing strand

    DNA polymerase catalyzes the addition of dNTPs to the free 3'-OH of the growing chain, reading the template 3'→5' and synthesizing 5'→3' with high fidelity.

  3. In the context of biochemistry, the term 'reducing sugar' refers to a sugar that:

    Answer: Contains a free anomeric hydroxyl group capable of acting as a reducing agent

    Reducing sugars have a free anomeric -OH group that can open to the aldehyde or keto form, allowing them to reduce oxidizing agents (e.g., Benedict's reagent, Fehling's solution).

  4. Which process describes the flow of genetic information according to the central dogma of molecular biology?

    Answer: DNA → RNA → Protein

    The central dogma states that genetic information flows from DNA (replication) → RNA (transcription) → Protein (translation), with reverse transcription as a special exception.

  5. Beta-oxidation of fatty acids occurs in which cellular location and produces which primary products?

    Answer: Mitochondrial matrix; acetyl-CoA, NADH, and FADH2

    Beta-oxidation in the mitochondrial matrix (and peroxisomes for very long-chain fatty acids) sequentially cleaves two-carbon units as acetyl-CoA while generating NADH and FADH2 for ATP production.

  6. Which of the following amino acids contains a sulfur atom in its side chain and forms disulfide bonds?

    Answer: Cysteine

    Cysteine's thiol (-SH) side chain can be oxidized to form disulfide (-S-S-) bonds with another cysteine, which are critical for protein tertiary and quaternary structure stabilization.