NEET-PG 2012 - Biochemistry Practice Questions

Q: What does Chargaff's rule state regarding the base pairing in DNA?

A=T, G=C. ***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.

Q: Which of the following statements is most specifically characteristic of mature cytoplasmic messenger RNA (mRNA) compared to its precursor?

Has a lower molecular weight than hn-RNA.. ***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.

Q: What is the rate-limiting enzyme in heme synthesis?

ALA synthase. ***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.

Q: The primary defect which leads to sickle cell anemia is:

Replacement of glutamate by valine in β-chain of HbA. ***Replacement of glutamate by valine in β-chain of HbA*** - The primary defect in sickle cell anemia is a **point mutation** that leads to the replacement of **glutamic acid** with **valine** in the **sixth position** of the β-globin chain [1]. - This mutation causes the hemoglobin (HbS) to polymerize under low oxygen conditions, resulting in the characteristic **sickle-shaped red blood cells** [1]. *A nonsence mutation in the I3-chain of HbA* - A nonsense mutation leads to a **premature stop codon**, which is not the mechanism behind sickle cell anemia. - This mutation does not involve the β-globin chain, which is critical in this specific disorder. *Substitution of valine by glutamate in the a-chain of HbA* - This statement is incorrect as sickle cell anemia specifically involves the **β-chain**, not the **α-chain**. - Substituting valine with glutamate does not cause sickling but rather the opposite of the actual defect observed in this condition. *An abnormality in porphyrin part of hemoglobin* - Sickle cell anemia does not arise from **porphyrin metabolism issues**, which are related to conditions like **porphyrias**. - The primary defect is a change in the amino acid sequence, not in the porphyrin structure of hemoglobin. **References:** [1] Cross SS. Underwood's Pathology: A Clinical Approach. 6th ed. Common Clinical Problems From Blood And Bone Marrow Disease, pp. 598-599.

Q: The cofactor vitamin B12 is required for the following conversion:

Methyl malonyl CoA to succinyl CoA. ***Methyl malonyl CoA to succinyl CoA*** - **Vitamin B12**, in its active form **adenosylcobalamin**, is a crucial cofactor for the enzyme **methylmalonyl-CoA mutase**, which catalyzes the isomerization of **methylmalonyl-CoA to succinyl-CoA**. - This conversion is vital for the metabolism of **odd-chain fatty acids** and certain **amino acids**, allowing their entry into the **Krebs cycle**. *Dopamine to Norepinephrine* - This conversion is catalyzed by **dopamine beta-hydroxylase**, which requires **vitamin C** (ascorbate) and **copper** as cofactors, not vitamin B12. - It is a key step in the synthesis of **catecholamines** within the nervous system. *Propionyl CoA to methyl malonyl CoA* - This conversion is catalyzed by **propionyl-CoA carboxylase** and requires **biotin** as a cofactor, not vitamin B12. - This reaction is the first step in the metabolic pathway that leads to succinyl-CoA from odd-chain fatty acids. *Homocysteine to cysteine* - This conversion occurs via the **transsulfuration pathway** and requires **vitamin B6** (pyridoxal phosphate) as a cofactor, not vitamin B12. - The enzymes involved are **cystathionine β-synthase** and **cystathionine γ-lyase**, both B6-dependent. - Vitamin B12 is involved in the **remethylation** of homocysteine to methionine (not in transsulfuration to cysteine).

Q: Which amino acids are involved in the formation of purines?

Aspartate, glycine, glutamine. ***Aspartate, glycine, glutamine*** - **Glycine** provides the largest single contribution to the purine ring structure: carbons at positions 4 and 5, and nitrogen at position 7 (the entire glycine molecule is incorporated). - **Aspartate** contributes the nitrogen atom at position 1 of the purine ring. - **Glutamine** donates two nitrogen atoms to the purine ring, specifically at positions 3 and 9. *Aspartate, glycine* - While both **aspartate** and **glycine** are crucial, **glutamine** is also required for the complete synthesis of the purine ring, contributing two nitrogen atoms. - Omission of glutamine makes this option incomplete for the full complement of amino acids involved. *Aspartate, glutamate* - **Glutamate** is not directly involved as an amino acid precursor contributing atoms to the purine ring structure. - **Glutamine**, an amide of glutamate, is the active donor of nitrogen atoms for purine synthesis. *Aspartic acid, glycine, uric acid* - **Aspartic acid** is another name for aspartate, and **glycine** is correctly identified as a precursor. - However, **uric acid** is the end product of purine catabolism, not an amino acid involved in its synthesis.

Q: The Watson-Crick model is for which type of DNA?

B DNA. ***B DNA*** - The **Watson-Crick model** describes the most common and stable form of DNA found in living organisms under physiological conditions. - **B-DNA** is a right-handed double helix, characterized by a **major and minor groove**, with approximately 10-10.5 base pairs per turn. *A DNA* - **A-DNA** is a **right-handed double helix** that forms under dehydrating conditions and is shorter and wider than B-DNA. - It has a more tilted base pair arrangement and is not the primary form described by the Watson-Crick model. *C DNA* - **C-DNA** is a less common **right-handed double helix** that forms under even lower hydration conditions and in the presence of certain ions. - It has fewer base pairs per turn than B-DNA, typically around 9.3 base pairs. *Z DNA* - **Z-DNA** is unique because it is a **left-handed double helix**, unlike the right-handed forms of A, B, and C DNA. - It is transiently formed in regions with a high concentration of **GC base pairs** and has a zigzag backbone, hence its name.

Q: Which of the following is a ribozyme?

Peptidyl transferase. ***Peptidyl transferase*** - This enzyme is an integral part of the **large ribosomal subunit** and is responsible for catalyzing the formation of peptide bonds during protein synthesis. - While historically thought to be purely proteinaceous, it is now known that the **catalytic activity** of peptidyl transferase comes from its **rRNA component**, specifically the 23S rRNA in prokaryotes and 28S rRNA in eukaryotes, making it a ribozyme. *Elongation factor 2* - **Elongation Factor 2 (EF2)** is a **GTPase** that facilitates the translocation of the ribosome along the mRNA during protein synthesis. - It is a **protein**, not an RNA molecule, and thus does not possess catalytic activity as a ribozyme. *Primase* - **Primase** is an **RNA polymerase** that synthesizes short RNA primers required for the initiation of DNA replication. - It is a **protein enzyme** and not an RNA molecule with catalytic activity. *RNA polymerase* - **RNA polymerase** is a **protein enzyme** responsible for synthesizing RNA from a DNA template during transcription. - It uses a DNA template to produce an RNA strand, but its own catalytic activity is derived from its **protein structure**, not from an RNA component.

Q: What is the primary function of exonuclease in DNA replication?

Proofreading. ***Proofreading*** - Exonucleases, particularly those associated with **DNA polymerases**, are crucial for **proofreading** during DNA replication. - They remove incorrectly paired nucleotides from the 3' end of the growing DNA strand, ensuring high fidelity of replication. *Polymerization* - **DNA polymerase** is primarily responsible for the **polymerization** of new DNA strands by adding nucleotides. - While exonucleases can be part of the polymerase complex, their main function is not polymerization itself. *Chain elongation* - **Chain elongation** refers to the process of adding nucleotides to the growing DNA strand, which is performed by **DNA polymerase**. - Exonucleases act as a quality control mechanism during this elongation process, rather than carrying out the elongation. *Termination* - **Termination** of DNA replication involves specific sequences and proteins that signal the end of replication, not the primary function of exonucleases. - Exonucleases are active throughout the replication process to maintain accuracy.

Q: In sickle cell anemia, the mutation at codon 6 results in the substitution of which amino acid?

Valine for glutamic acid. ***Valine for glutamic acid*** - In **sickle cell anemia**, the normal **glutamic acid** at codon 6 of the $\beta$-globin chain is replaced by **valine**. - This single amino acid substitution is responsible for the abnormal **hemoglobin S (HbS)** and the characteristic sickling of red blood cells. *Isoleucine for valine* - This substitution is **not characteristic** of sickle cell anemia. - While other hemoglobinopathies exist, this specific change does not lead to the sickle cell phenotype. *Valine for isoleucine* - This substitution is **not the primary genetic defect** found in sickle cell anemia. - The mutation in sickle cell anemia involves the replacement of a negatively charged amino acid with a neutral one. *Glutamic acid for valine* - This represents the **reverse substitution** of what occurs in sickle cell anemia. - In sickle cell, valine replaces glutamic acid, not the other way around.

Question 1

What does Chargaff's rule state regarding the base pairing in DNA?

Accepted Answer

A=T, G=C

Answer

A=G, T=C

Answer

A=C, G=T

Answer

Any combination possible

Question 2

Which of the following statements is most specifically characteristic of mature cytoplasmic messenger RNA (mRNA) compared to its precursor?

Accepted Answer

Has a lower molecular weight than hn-RNA.

Answer

Transcribed from nuclear DNA.

Answer

Contains uracil instead of thymine.

Answer

Sugar is ribose.

Question 3

What is the rate-limiting enzyme in heme synthesis?

Accepted Answer

ALA synthase

Answer

HMG CoA reductase

Answer

ALA dehydratase

Answer

Uroporphyrinogen 1 synthase

Question 4

The primary defect which leads to sickle cell anemia is:

Accepted Answer

Replacement of glutamate by valine in β-chain of HbA

Answer

An abnormality in porphyrin part of hemoglobin

Answer

A nonsense mutation in the β-chain of HbA

Answer

Substitution of valine by glutamate in the α-chain of HbA

Question 5

The cofactor vitamin B12 is required for the following conversion:

Accepted Answer

Methyl malonyl CoA to succinyl CoA

Answer

Dopamine to Norepinephrine

Answer

Propionyl CoA to methyl malonyl CoA

Answer

Homocysteine to cysteine

Question 6

Which amino acids are involved in the formation of purines?

Accepted Answer

Aspartate, glycine, glutamine

Answer

Aspartate, glycine

Answer

Aspartate, glutamate

Answer

Aspartic acid, glycine, uric acid

Question 7

The Watson-Crick model is for which type of DNA?

Accepted Answer

B DNA

Answer

A DNA

Answer

C DNA

Answer

Z DNA

Question 8

Which of the following is a ribozyme?

Accepted Answer

Peptidyl transferase

Answer

Elongation factor 2

Answer

Primase

Answer

RNA polymerase

Question 9

What is the primary function of exonuclease in DNA replication?

Accepted Answer

Proofreading

Answer

Polymerization

Answer

Chain elongation

Answer

Termination

Question 10

In sickle cell anemia, the mutation at codon 6 results in the substitution of which amino acid?

Accepted Answer

Valine for glutamic acid

Answer

Isoleucine for valine

Answer

Valine for isoleucine

Answer

Glutamic acid for valine

NEET-PG 2012 — Biochemistry