What is attached to the 3' end of mRNA after transcription?
What does Chargaff's rule state regarding the base pairing in DNA?
Which of the following statements is most specifically characteristic of mature cytoplasmic messenger RNA (mRNA) compared to its precursor?
What is the rate-limiting enzyme in heme synthesis?
The anticodon region is an important part of which type of RNA?
What is the classification of the Y chromosome?
What cofactor is required for the proper functioning of glucose-6-phosphate dehydrogenase?
Apoenzyme is ?
Enzyme causing covalent bond cleavage without hydrolysis ?
How do enzymes function in biochemical reactions?
NEET-PG 2012 - Biochemistry NEET-PG Practice Questions and MCQs
Question 61: What is attached to the 3' end of mRNA after transcription?
- A. CCA
- B. Intron
- C. 7-methylguanosine
- D. Poly-A tail (Correct Answer)
Explanation: ***Poly-A tail*** - A **poly-A tail**, consisting of multiple adenosine monophosphates, is added to the **3' end of mRNA** after transcription to protect it from degradation. - This modification aids in the **transport of mRNA from the nucleus to the cytoplasm** and in its translation. *CCA* - The **CCA sequence** is found at the **3' end of tRNA**, not mRNA, and is critical for amino acid attachment. - It is added post-transcriptionally to tRNA molecules by the enzyme **tRNA nucleotidyltransferase**. *Intron* - **Introns** are non-coding regions within a gene that are transcribed into mRNA but are subsequently removed during **RNA splicing**, not added to the 3' end. - Their removal ensures that only the **coding regions (exons)** are translated into protein. *7-methylguanosine* - **7-methylguanosine** forms the **5' cap** of mRNA, which is added to the 5' end, not the 3' end. - This cap is important for **mRNA stability**, ribosome binding, and protection against degradation.
Question 62: What does Chargaff's rule state regarding the base pairing in DNA?
- A. A=T, G=C (Correct Answer)
- B. A=G, T=C
- C. A=C, G=T
- D. Any combination possible
Explanation: ***A=T, G=C*** - **Chargaff's rules** state that in any double-stranded DNA, the amount of **adenine (A)** is approximately equal to the amount of **thymine (T)**, and the amount of **guanine (G)** is approximately equal to the amount of **cytosine (C)**. - This equivalency reflects the specific **base pairing** in the DNA double helix, where A always pairs with T, and G always pairs with C. *A=G, T=C* - This statement is incorrect as it proposes an atypical and biologically inaccurate pairing between a **purine (A)** and another **purine (G)**, and a **pyrimidine (T)** with a **pyrimidine (C)**. - This combination would disrupt the uniform diameter of the DNA double helix required for its structural stability. *A=C, G=T* - This option is incorrect because it suggests pairing a purine (A) with a pyrimidine (C) and a purine (G) with a pyrimidine (T) in a way that is not observed in natural DNA. - Such pairings would also lead to an irregular width of the DNA molecule, destabilizing its structure. *Any combination possible* - This statement is false; base pairing in DNA is **highly specific** and not random due to chemical and structural constraints. - The specific pairing rules (**A with T, G with C**) are crucial for maintaining the consistent structure of the DNA double helix and for accurate DNA replication and transcription.
Question 63: Which of the following statements is most specifically characteristic of mature cytoplasmic messenger RNA (mRNA) compared to its precursor?
- A. Transcribed from nuclear DNA.
- B. Has a lower molecular weight than hn-RNA. (Correct Answer)
- C. Contains uracil instead of thymine.
- D. Sugar is ribose.
Explanation: ***Has a lower molecular weight than hn-RNA.*** - **Mature mRNA** undergoes **splicing**, which removes **introns** (non-coding regions) from the heterogeneous nuclear RNA (hnRNA) precursor. - The removal of these introns results in a **shorter, more compact molecule** with a lower molecular weight compared to the original hnRNA. *Transcribed from nuclear DNA.* - While mRNA is indeed **transcribed from DNA**, this statement is true for **all types of RNA (rRNA, tRNA, and mRNA)**, not just mature cytoplasmic mRNA specifically, and does not differentiate it. - The initial transcript is **hnRNA**, which is then processed into mature mRNA. *Contains uracil instead of thymine.* - This is a characteristic of **all RNA molecules**, not just mature cytoplasmic mRNA, and is a fundamental difference between RNA and DNA. - DNA contains **thymine**, while RNA contains **uracil**. *Sugar is ribose.* - This is a distinguishing feature of **all RNA molecules**, indicating that the sugar component of its nucleotides is **ribose**, whereas DNA contains **deoxyribose**. - This statement is not unique to mature cytoplasmic mRNA.
Question 64: What is the rate-limiting enzyme in heme synthesis?
- A. ALA synthase (Correct Answer)
- B. HMG CoA reductase
- C. ALA dehydratase
- D. Uroporphyrinogen 1 synthase
Explanation: ***ALA synthase*** - **Aminolevulinate synthase** (ALA synthase) is the first and **rate-limiting enzyme** in the heme synthesis pathway. - Its activity is tightly regulated, and its overexpression or deficiency can lead to disorders like **acute intermittent porphyria**. *Hmg coa reductase* - **HMG-CoA reductase** is the **rate-limiting enzyme** in the **cholesterol biosynthesis pathway**, not heme synthesis. - It is the target enzyme for statin medications, which lower cholesterol levels. *ALA dehydratase* - **ALA dehydratase** (also known as porphobilinogen synthase) is the second enzyme in the heme synthesis pathway, responsible for converting two molecules of **ALA to porphobilinogen**. - While critical, it is not the rate-limiting step; inhibition of this enzyme can lead to **lead poisoning**. *Uroporphyrinogen 1 synthase* - **Uroporphyrinogen I synthase** (also called hydroxymethylbilane synthase or porphobilinogen deaminase) catalyzes the formation of **hydroxymethylbilane** from four molecules of **porphobilinogen**. - A deficiency in this enzyme is associated with **acute intermittent porphyria**, but it is not the rate-limiting enzyme of the overall pathway.
Question 65: The anticodon region is an important part of which type of RNA?
- A. r-RNA
- B. m-RNA
- C. t-RNA (Correct Answer)
- D. hn-RNA
Explanation: **t-RNA** - The **anticodon region** is a critical component of **transfer RNA (tRNA)**, responsible for recognizing and binding to the complementary codon on mRNA during protein synthesis. - This interaction ensures that the correct **amino acid** is delivered to the growing polypeptide chain according to the genetic code. *r-RNA* - **Ribosomal RNA (rRNA)** is a structural and enzymatic component of **ribosomes**, which are the cellular machinery for protein synthesis. - While rRNA plays a crucial role in forming **peptide bonds** and facilitating translation, it does not possess an anticodon region. *m-RNA* - **Messenger RNA (mRNA)** carries the **genetic code** from DNA to the ribosomes in the form of codons, which specify the sequence of amino acids for protein synthesis. - mRNA molecules have codons, but they do not have an **anticodon region**; instead, they are read by the anticodons of tRNA. *hn-RNA* - **Heterogeneous nuclear RNA (hnRNA)** is a precursor to mRNA in eukaryotic cells, containing both exons and introns. - It undergoes extensive processing, including **splicing**, to become mature mRNA, but it does not have an **anticodon region**.
Question 66: What is the classification of the Y chromosome?
- A. Metacentric
- B. Submetacentric (Correct Answer)
- C. Acrocentric
- D. None of the options
Explanation: ***Submetacentric*** - The **Y chromosome** is classified as submetacentric because its **centromere** is located off-center, resulting in two arms of unequal length. - The short arm (Yp) is smaller than the long arm (Yq), but not as disproportionate as in acrocentric chromosomes. - The **X chromosome** is also submetacentric, making both sex chromosomes belong to this category. *Metacentric* - A **metacentric chromosome** has its **centromere** located in the middle, resulting in two arms of approximately equal length. - Examples include chromosomes 1, 3, 16, 19, and 20, which have nearly equal arm ratios unlike the Y chromosome. *Acrocentric* - An **acrocentric chromosome** has its **centromere** located very close to one end, creating one very short arm and one very long arm. - The five acrocentric human chromosomes are **13, 14, 15, 21, and 22**, which possess satellite DNA and nucleolar organizing regions (NORs) on their short arms. - The **Y chromosome is NOT acrocentric** despite historical confusion; it has a more centrally positioned centromere than true acrocentric chromosomes. *None of the options* - This option is incorrect because the Y chromosome has a specific and well-established classification as **submetacentric** based on its centromere position and arm ratio.
Question 67: What cofactor is required for the proper functioning of glucose-6-phosphate dehydrogenase?
- A. NAD
- B. NADP (Correct Answer)
- C. FAD
- D. FMN
Explanation: ***NADP*** - **NADP+** (nicotinamide adenine dinucleotide phosphate) acts as the **electron acceptor** in the **glucose-6-phosphate dehydrogenase (G6PD)** reaction, becoming **NADPH**. - **NADPH** is crucial for maintaining the **redox balance** in cells, particularly in red blood cells, by reducing **oxidative stress**. *NAD* - **NAD+** (nicotinamide adenine dinucleotide) is a primary cofactor for many **dehydrogenase reactions** in catabolic pathways like **glycolysis** and the **Krebs cycle**. - It primarily functions as an electron acceptor in pathways that generate **ATP**, distinct from the role of **NADPH** in reductive biosynthesis and antioxidant defense. *FAD* - **FAD** (flavin adenine dinucleotide) is a coenzyme derived from **riboflavin (vitamin B2)** that is involved in various redox reactions, often in the form of **flavoproteins**. - Enzymes like **succinate dehydrogenase** in the electron transport chain utilize **FAD** as an electron acceptor, which is not the case for G6PD. *FMN* - **FMN** (flavin mononucleotide) is another coenzyme derived from **riboflavin**, structurally similar to FAD but lacking the additional adenosine monophosphate. - It participates in electron transfer reactions, particularly within **complex I** of the **electron transport chain**, but is not a cofactor for G6PD.
Question 68: Apoenzyme is ?
- A. Protein moiety (Correct Answer)
- B. Organic cofactor
- C. Inactive enzyme component
- D. Non-protein component required for enzyme activity
Explanation: ***Protein moiety*** - An **apoenzyme** is the **protein component of an enzyme** that is catalytically inactive by itself. - It requires a **non-protein cofactor** (either an inorganic ion or an organic molecule) to become active. *Organic cofactor* - An **organic cofactor** is also known as a **coenzyme**, which binds to the apoenzyme to form a functional holoenzyme. - While essential for enzyme activity, the apoenzyme itself is the protein part, not the organic cofactor. *Inactive enzyme component* - While an apoenzyme is **inactive on its own**, this description is too broad and doesn't specify its chemical nature. - It is specifically the **protein component** that is inactive until bound to its cofactor. *Non-protein component required for enzyme activity* - This describes a **cofactor** (either inorganic or organic), not the apoenzyme itself. - The apoenzyme is the **protein portion**, which *requires* the non-protein component for activity.
Question 69: Enzyme causing covalent bond cleavage without hydrolysis ?
- A. Lyase (Correct Answer)
- B. Ligase
- C. Hydrolase
- D. Transferase
Explanation: ***Lyase*** - **Lyases** are enzymes that catalyze the cleavage of **covalent bonds** (C-C, C-O, C-N, and others) by means other than hydrolysis or oxidation, often creating a new double bond or a ring structure. - They remove groups from substrates to form double bonds, or conversely, add groups to double bonds. - **Examples:** Aldolase (cleaves C-C bonds in glycolysis), carbonic anhydrase (reversible cleavage of C-O bond), fumarase (C-C bond cleavage in TCA cycle). *Ligase* - **Ligases** are enzymes that join two large molecules by forming a new chemical bond, usually accompanied by the **hydrolysis of ATP**. - They are involved in synthesis reactions, not the cleavage of bonds. *Hydrolase* - **Hydrolases** specifically catalyze the hydrolysis of a chemical bond, involving the **addition of water** across the bond. - They break down large molecules into smaller ones using water - this is the key difference from lyases. *Transferase* - **Transferases** catalyze the transfer of a **functional group** from one molecule (the donor) to another (the acceptor). - They do not cause covalent bond cleavage without hydrolysis but rather move existing groups between molecules.
Question 70: How do enzymes function in biochemical reactions?
- A. Increase in activation energy
- B. Decrease in activation energy (Correct Answer)
- C. Shift equilibrium constant
- D. Provide energy to the reaction
Explanation: ***Decrease in activation energy*** - Enzymes act as **biological catalysts** by providing an alternative reaction pathway with a lower **transition state energy**. - This reduction in the **activation energy** allows a higher proportion of reactant molecules to overcome the energy barrier and react, thereby increasing the reaction rate. *Increase in activation energy* - This statement is incorrect as increasing activation energy would slow down the reaction rate, which is contrary to the function of enzymes. - Enzymes are designed to accelerate reactions, not inhibit them, by making them energetically more favorable to proceed. *Shift equilibrium constant* - Enzymes catalyze both the forward and reverse reactions equally, meaning they accelerate the rate at which equilibrium is reached but **do not alter the equilibrium constant (Keq)** of a reaction. - The equilibrium constant is determined by the difference in free energy between reactants and products, which enzymes do not change. *Provide energy to the reaction* - This statement is incorrect because enzymes do **not provide energy** to reactions; they only lower the activation energy barrier. - Enzymes facilitate reactions by stabilizing the transition state, not by adding energy to the system, which would violate thermodynamic principles.