NEET-PG 2012 Practice Questions

Q: Which amino acid requires ascorbic acid for its formation in the body?

Hydroxyproline. ***Hydroxyproline*** - **Ascorbic acid (Vitamin C)** is an essential cofactor for **prolyl hydroxylase** and **lysyl hydroxylase** enzymes - These enzymes catalyze the **post-translational hydroxylation** of proline and lysine residues within collagen chains to form hydroxyproline and hydroxylysine - This hydroxylation is crucial for **stabilization of the collagen triple helix** structure - Hydroxyproline is formed by **modification of proline after incorporation into collagen**, not as a free amino acid - **Scurvy** (Vitamin C deficiency) results in defective collagen due to inadequate hydroxyproline formation *Lysine* - Lysine is an **essential amino acid** obtained from diet - Does not require ascorbic acid for its synthesis or formation - While lysine residues in collagen can be hydroxylated (forming hydroxylysine), the question asks about the amino acid whose formation requires Vitamin C *Cysteine* - Cysteine is a **sulfur-containing amino acid** synthesized from methionine via transsulfuration pathway - Its synthesis does not involve ascorbic acid *Proline* - Proline is a **non-essential amino acid** synthesized from glutamate - **Proline synthesis does not require ascorbic acid** - Proline serves as the precursor that gets hydroxylated to hydroxyproline within collagen

Q: Which of the following requires vitamin B12?

Conversion of homocysteine to methionine. ***Homocysteine to methionine*** - The conversion of **homocysteine to methionine** is catalyzed by **methionine synthase**, an enzyme that requires **vitamin B12** (cobalamin) as a cofactor. - **Vitamin B12** facilitates the transfer of a methyl group from **methyltetrahydrofolate** to homocysteine, forming methionine. *Conversion of serine to lysine* - The metabolism of **serine to lysine** involves multiple steps and different enzymes, but it does not directly require **vitamin B12**. - Lysine is an **essential amino acid** and is primarily obtained from dietary sources or synthesized through complex pathways. *Conversion of serine to glycine* - The conversion of **serine to glycine** is catalyzed by **serine hydroxymethyltransferase**, which requires **tetrahydrofolate (THF)** as a cofactor, not vitamin B12. - This reaction generates **5,10-methylenetetrahydrofolate**, an important one-carbon donor. *Conversion of glutamine to glutamate* - The conversion of **glutamine to glutamate** is primarily catalyzed by **glutaminase**, an enzyme that does not require **vitamin B12**. - This reaction involves the removal of an **ammonia group** from glutamine to form glutamate.

Q: Which of the following micronutrient deficiencies can lead to anemia?

Copper. ***Copper*** - **Copper** is essential for **iron metabolism** and red blood cell formation; its deficiency can lead to **sideroblastic anemia** (often with microcytic or normocytic features) that may be accompanied by neutropenia. - Copper is required for **ceruloplasmin** function, which is necessary for iron mobilization from stores and incorporation into hemoglobin. - It also plays a role in the function of **superoxide dismutase** and **cytochrome c oxidase**, enzymes involved in antioxidant defense and energy production. *Molybdenum* - **Molybdenum** is a cofactor for several enzymes, including **xanthine oxidase** and **sulfite oxidase**, crucial for purine metabolism and detoxification. - While essential, its deficiency does not typically lead to **anemia** in humans. *Selenium* - **Selenium** is a component of selenoproteins, such as **glutathione peroxidase**, which protect cells from oxidative damage. - Deficiency is associated with conditions like **Keshan disease** (cardiomyopathy) but not primary anemia. *Fluorine* - **Fluorine** (as fluoride) is primarily known for its role in **bone and tooth mineralization**, protecting against dental caries. - It does not directly participate in **hematopoiesis** or iron metabolism, and its deficiency is not linked to anemia.

Q: What is the primary function of reverse transcription?

Synthesis of DNA from an RNA template. ***Synthesis of DNA from an RNA template*** - **Reverse transcription** is catalyzed by the enzyme **reverse transcriptase**, which uses an **RNA template** to synthesize a complementary DNA (cDNA) strand. - This process is fundamental in the life cycle of **retroviruses** like HIV, allowing them to integrate their genetic material into the host genome. *Synthesis of RNA from a DNA template* - This process is known as **transcription**, where genetic information is copied from **DNA to RNA**, not the reverse. - It is a key step in gene expression, leading to the production of various types of RNA molecules. *Synthesis of DNA from a DNA template* - This describes **DNA replication**, the process by which DNA makes copies of itself, ensuring genetic continuity during cell division. - It involves enzymes like **DNA polymerase** and creates two identical DNA molecules from one original DNA molecule. *Synthesis of RNA from an RNA template* - This process is known as **RNA replication** and is characteristic of certain **RNA viruses** (e.g., influenza virus), where RNA serves as both the template and the genetic material. - It involves an enzyme called **RNA-dependent RNA polymerase**.

Q: Which of the following usually require a RNA intermediate for cloning/replication?

Retroviruses. ***Retroviruses*** - **All retroviruses require an RNA intermediate** for their replication cycle, making this the correct answer. - Retroviruses have an **RNA genome** that must be **reverse transcribed into DNA** by reverse transcriptase enzyme before integration into the host genome. - The integrated DNA (provirus) is then transcribed back to RNA, which serves both as mRNA for viral proteins and as genomic RNA for new virions. - Examples include **HIV, HTLV**, and other retroviruses that definitively use this RNA → DNA → RNA replication strategy. *Transposons* - This option is **too broad** to be correct. Only **retrotransposons** (Class I transposons) use RNA intermediates via a "copy-and-paste" mechanism involving reverse transcription. - However, **DNA transposons** (Class II) move by a "cut-and-paste" DNA mechanism **without any RNA intermediate**. - Since the question asks what "usually requires" RNA intermediate, and many common transposons (like bacterial Tn5, Tn10) are DNA transposons, this answer is imprecise. *Cosmids* - Cosmids are **hybrid cloning vectors** containing cos sites from bacteriophage lambda combined with plasmid sequences. - They replicate as **DNA plasmids** in bacteria using DNA-dependent DNA polymerase. - No RNA intermediate is involved in their replication mechanism. *Plasmids* - Plasmids are **extrachromosomal circular DNA molecules** that replicate independently within bacterial or yeast cells. - Replication occurs via **DNA-to-DNA synthesis** using DNA polymerase. - No RNA intermediate is required for plasmid propagation.

Q: Which of the following is a termination codon?

UAA. ***UAA*** - **UAA** is one of the three **stop codons** (UAA, UAG, UGA) that signals the termination of protein synthesis during translation. - When the ribosome encounters a UAA codon, no corresponding tRNA with an anticodon binds, and release factors bind instead, leading to the dissociation of the polypeptide chain. *AUG* - **AUG** is the universal **start codon** in most organisms, encoding for methionine in eukaryotes and N-formylmethionine in prokaryotes. - Its presence signals the initiation of protein synthesis, not its termination. *AUA* - **AUA** is a codon that codes for the amino acid **Isoleucine**. - It is a **sense codon** and does not act as a signal for termination. *AGG* - **AGG** is a codon that codes for the amino acid **Arginine**. - Similar to AUA, it is a **sense codon** and participates in elongating the polypeptide chain, rather than terminating it.

Q: Protein refolding is carried out by?

Chaperone. ***Chaperone*** - **Chaperone proteins** assist in the proper folding of other proteins, particularly during stress conditions like heat shock, by preventing **aggregation** and promoting correct conformation. - They do not become part of the final functional protein but transiently bind during the folding process, thus facilitating **protein refolding** and assembly. *Valine* - **Valine** is an **essential amino acid** and a building block for proteins, but it does not play a direct role in protein refolding. - It contributes to the **hydrophobic core** of proteins due to its non-polar side chain, influencing protein structure but not managing the folding process. *Threonine* - **Threonine** is an **essential amino acid** with a polar side chain, often involved in **glycosylation** and phosphorylation, but not in the complex process of protein refolding. - Its hydroxyl group can participate in **hydrogen bonding**, influencing protein stability and interactions, but not acting as a folding catalyst. *Aspartate* - **Aspartate** is a **non-essential acidic amino acid** that can be involved in various metabolic pathways and is a component of proteins. - Its acidic side chain can form **salt bridges** and hydrogen bonds, contributing to the protein's overall charge and structure, but it does not actively oversee protein refolding.

Q: Where does oxidative deamination primarily occur in the human body?

Mitochondria of liver cells. ***Mitochondria of liver cells*** - **Oxidative deamination**, particularly of glutamate, is a central process in **amino acid catabolism** and occurs predominantly in the **mitochondria of liver cells**. - This process is crucial for removing the **amino group (NH3)** from amino acids, forming ammonia, which is then detoxified into urea. *Cytoplasm of all cells* - While cells have cytoplasmic metabolic pathways, the primary enzyme for oxidative deamination, **glutamate dehydrogenase**, is located in the mitochondria. - The cytoplasm primarily handles glycolysis and various synthetic pathways, but not the bulk of oxidative deamination. *Mitochondria of all cells* - Although mitochondria are the site of oxidative metabolism in most cells, the **liver** is the main organ responsible for processing exogenous amino acids and their subsequent comprehensive deamination. - Other cells perform some amino acid metabolism, but not the large-scale oxidative deamination seen in the liver. *Cytoplasm of liver cells* - The cytoplasm of liver cells is involved in various metabolic processes, including gluconeogenesis and fatty acid synthesis. - However, the key enzymes for oxidative deamination are specifically compartmentalized within the **mitochondria** of these cells, not the cytoplasm.

Q: What color is emitted by FITC after absorbing blue light?

Yellow-green. ***Yellow-green*** - Fluorescein isothiocyanate (FITC) is a common fluorochrome used in **fluorescence microscopy** and flow cytometry. - Upon excitation by blue light (typically around 495 nm), FITC emits light in the **yellow-green spectrum**, specifically around 521 nm. - This is the **spectroscopically accurate** description of FITC's emission peak. *Orange-red* - **Orange-red emission** is characteristic of fluorochromes like **phycoerythrin (PE)** or **Texas Red**, not FITC. - These fluorochromes have different **excitation and emission maxima** compared to FITC. *Apple-green* - While FITC fluorescence is sometimes clinically described as **"apple-green"** (especially in immunofluorescence), this is a **subjective visual description** rather than a precise spectral term. - The more **spectroscopically accurate** description is **yellow-green**, which reflects FITC's specific emission peak at 521 nm. - "Apple-green" typically suggests a purer green without the yellow component. *Golden-brown* - **Golden-brown** is not a typical emission color for fluorochromes like FITC. - This color is generally associated with **pigments** or stained tissues (e.g., lipofuscin, hemosiderin), not fluorescent probes.

Question 1

Which amino acid requires ascorbic acid for its formation in the body?

Accepted Answer

Hydroxyproline

Answer

Lysine

Answer

Cysteine

Answer

Proline

Question 2

Which of the following requires vitamin B12?

Accepted Answer

Conversion of homocysteine to methionine

Answer

Conversion of serine to lysine

Answer

Conversion of serine to glycine

Answer

Conversion of glutamine to glutamate

Question 3

Which of the following micronutrient deficiencies can lead to anemia?

Accepted Answer

Copper

Answer

Molybdenum

Answer

Fluorine

Answer

Selenium

Question 4

What is the function of DNA ligase?

Accepted Answer

Joins the Okazaki fragments on the lagging strand by sealing the nicks between them.

Answer

Unwinding (denaturation) of dsDNA to provide an ssDNA template

Answer

Initiation of DNA synthesis and elongation

Answer

Initiates synthesis of RNA primers

Question 5

What is the primary function of reverse transcription?

Accepted Answer

Synthesis of DNA from an RNA template

Answer

Synthesis of RNA from a DNA template

Answer

Synthesis of DNA from a DNA template

Answer

Synthesis of RNA from an RNA template

Question 6

Which of the following usually require a RNA intermediate for cloning/replication?

Accepted Answer

Retroviruses

Answer

Cosmids

Answer

Plasmids

Answer

Transposons

Question 7

Which of the following is a termination codon?

Accepted Answer

UAA

Answer

AUG

Answer

AUA

Answer

AGG

Question 8

Protein refolding is carried out by?

Accepted Answer

Chaperone

Answer

Valine

Answer

Threonine

Answer

Aspartate

Question 9

Where does oxidative deamination primarily occur in the human body?

Accepted Answer

Mitochondria of liver cells

Answer

Cytoplasm of all cells

Answer

Mitochondria of all cells

Answer

Cytoplasm of liver cells

Question 10

What color is emitted by FITC after absorbing blue light?

Accepted Answer

Yellow-green

Answer

Orange-red

Answer

Apple-green

Answer

Golden-brown

NEET-PG 2012

Biochemistry

Pathology