NEET-PG 2015 Practice Questions

Q: Which of the following statements is true regarding the functions of cAMP and cGMP?

They are both second messengers.. ***They are both second messengers.*** - **cAMP (cyclic adenosine monophosphate)** and **cGMP (cyclic guanosine monophosphate)** are crucial intracellular signaling molecules. - They relay signals from **first messengers** (like hormones or neurotransmitters) received at the cell surface to intracellular targets, thus acting as second messengers. *They act on membrane receptors.* - **cAMP** and **cGMP** are *produced* in response to activation of **membrane receptors** by first messengers, but they themselves do not act directly on these receptors. - Their action is primarily *intracellular*, binding to and activating various enzymes and proteins like **protein kinases**. *All of the above statements are true* - This statement is incorrect because the claim that they act on membrane receptors is false. - Only one of the statements provided is accurate regarding the functions of cAMP and cGMP. *They act by post-translational modification.* - While cAMP and cGMP can lead to **post-translational modification** (e.g., phosphorylation by protein kinases A and G), they are not themselves the direct modifiers. - They act as **allosteric regulators** of enzymes, which then catalyze the modifications.

Q: Which of the following compounds is not formed with the involvement of glycine?

Thyroxine. ***Thyroxine*** - **Thyroxine** (and other thyroid hormones) are derived from the amino acid **tyrosine**. - Their synthesis involves iodination and coupling reactions of tyrosine residues within the protein **thyroglobulin**. *Heme* - **Glycine** is a direct precursor for the initial step in **heme synthesis**. - It condenses with **succinyl CoA** to form α-amino-β-ketoadipate, which then decarboxylates to form δ-aminolevulinate (ALA). *Purines* - **Glycine** contributes part of its structure to the **purine ring**. - Specifically, the **nitrogen at position 7** and the **carbons at positions 4 and 5** of the purine ring are derived from glycine. *Glutathione* - **Glutathione** is a tripeptide composed of three amino acids: **glutamate**, **cysteine**, and **glycine**. - **Glycine** is the C-terminal amino acid of glutathione and is essential for its structure and function as an antioxidant.

Q: Abnormal proteins which are bound to ubiquitin are degraded in -

Proteasomes. ***Proteasomes*** - **Proteasomes** are multi-subunit protein complexes responsible for degrading **ubiquitin-tagged proteins**. - This degradation is a tightly regulated process essential for cell cycle control, gene expression, and immune response. *Golgi apparatus* - The **Golgi apparatus** primarily functions in modifying, sorting, and packaging proteins and lipids synthesized in the Endoplasmic Reticulum. - It does not directly participate in the degradation of **ubiquitin-bound proteins**. *Smooth ER* - The **smooth endoplasmic reticulum (SER)** is involved in lipid synthesis, detoxification of drugs and poisons, and storage of calcium ions. - It lacks ribosomes and is not directly implicated in the degradation of misfolded proteins tagged with ubiquitin. *Lysosomes* - **Lysosomes** are organelles containing various hydrolytic enzymes that break down waste materials and cellular debris, as well as foreign invaders like bacteria. - While they degrade proteins, they primarily target **extracellular proteins** taken up by endocytosis or cellular components via **autophagy**, not specifically ubiquitin-bound proteins.

Q: Coenzyme for phenylalanine hydroxylase is?

Tetrahydrobiopterin. ***Tetrahydrobiopterin*** - **Tetrahydrobiopterin (BH4)** is an essential coenzyme for aromatic amino acid hydroxylases, including **phenylalanine hydroxylase (PAH)**. - PAH converts **phenylalanine** to **tyrosine**, and deficiencies in BH4 or PAH itself lead to *phenylketonuria (PKU)*. *Tetrahydrofolate* - **Tetrahydrofolate (THF)** is a coenzyme derived from **folic acid** and is primarily involved in **one-carbon metabolism**, including **purine** and **pyrimidine synthesis**, and various amino acid interconversions. - It does not directly act as a coenzyme for phenylalanine hydroxylase. *Pyridoxal phosphate* - **Pyridoxal phosphate (PLP)**, a derivative of **vitamin B6**, is a crucial coenzyme for many enzymes involved in **amino acid metabolism**, particularly in **transamination**, **decarboxylation**, and side-chain cleavage reactions. - It is not the coenzyme for phenylalanine hydroxylase. *S-adenosyl methionine* - **S-adenosyl methionine (SAM)** is a major **methyl donor** in various biochemical reactions, important for the synthesis of **neurotransmitters**, **hormones**, and **phospholipids**. - While essential for many metabolic pathways, it is not involved as a coenzyme for phenylalanine hydroxylase.

Q: GlcNAc-P-P-oligosaccharide is -

Glycoprotein. ***Glycoprotein*** - **GlcNAc-P-P-oligosaccharide** refers to the **N-linked oligosaccharide precursor** that is synthesized on a **dolichol pyrophosphate** carrier (`-P-P`). This complex is characteristic of the initial stages of **N-linked glycosylation**, a process that forms glycoproteins. - **N-acetylglucosamine (GlcNAc)** is a crucial sugar residue found at the reducing end of this precursor, linking it to the dolichol carrier. *Proteoglycan* - Proteoglycans consist of a **core protein** covalently attached to long, unbranched **glycosaminoglycan (GAG)** chains, such as chondroitin sulfate or heparin. - While they contain sugar units, their structure and synthesis pathway are distinct from the GlcNAc-P-P-oligosaccharide described, which is specific to N-linked glycoprotein synthesis. *Collagen* - **Collagen** is a fibrous protein, primarily composed of a triple helix of polypeptide chains rich in **glycine, proline, and hydroxyproline**. - Although collagen undergoes some post-translational modifications like **glycosylation**, it does not involve the GlcNAc-P-P-oligosaccharide precursor in its typical synthesis. *Phospholipid* - **Phospholipids** are a major component of cell membranes, composed of a **hydrophilic head** (containing a phosphate group) and two **hydrophobic fatty acid tails**. - They are lipids and do not contain carbohydrate structures like GlcNAc-P-P-oligosaccharide.

Q: Prolyl hydroxylase requires which cofactor?

Vitamin C. ***Vitamin C*** - **Prolyl hydroxylase** is an enzyme critical for the hydroxylation of proline residues during **collagen synthesis**. - **Vitamin C** (ascorbic acid) acts as an essential **cofactor**, reducing the ferric iron of the enzyme back to its ferrous state after each catalytic cycle, enabling continued activity. - The enzyme requires both **iron (Fe²⁺)** as a metal cofactor and **vitamin C** to maintain the iron in its reduced state. *Iron (Fe²⁺)* - While **iron** is indeed required by prolyl hydroxylase as a **metal cofactor**, the question asks for the cofactor, which specifically refers to **vitamin C**. - Iron functions as part of the enzyme's active site, but vitamin C is the reducing agent that keeps iron functional. - Vitamin C deficiency (scurvy) leads to defective collagen synthesis despite adequate iron. *Molybdenum* - **Molybdenum** is a cofactor for several human enzymes, including **xanthine oxidase** and **sulfite oxidase**. - However, it plays no direct role in the activity of prolyl hydroxylase. *Vitamin K1* - **Vitamin K1** is a crucial cofactor for **gamma-glutamyl carboxylase**, an enzyme involved in the carboxylation of glutamic acid residues in clotting factors. - It is not involved in the hydroxylation of proline by prolyl hydroxylase.

Q: What type of bond is involved in the side chain linkage of proteoglycans?

Covalent. ***Covalent*** - Proteoglycans are formed by **glycosaminoglycan (GAG)** chains that are covalently linked to a protein core. - Specifically, an **O-glycosidic bond** forms between a xylose residue on the GAG chain and a serine residue on the core protein. *Hydrogen bond* - **Hydrogen bonds** are weaker intermolecular forces that stabilize protein secondary structures and interactions between water molecules. - They are not strong enough to form the primary structural linkage between the GAG chains and the core protein in proteoglycans. *Electrostatic bond* - **Electrostatic bonds**, or ionic bonds, involve attraction between oppositely charged ions. While proteoglycans have many charged groups, these bonds are not the primary linkage connecting the GAG chains to the protein core. - They contribute to the overall structure and interactions of proteoglycans with other molecules but do not form the main side chain linkage. *Van-der Waal's force* - **Van der Waals forces** are weak, short-range intermolecular forces that arise from temporary fluctuations in electron distribution. - These forces play a role in tertiary and quaternary protein structure and molecular packing, but they are far too weak to establish the covalent attachments of GAG chains to the proteoglycan core protein.

Q: Creatinine is formed from -

Creatine. ***Creatine*** - **Creatinine** is a waste product formed from the non-enzymatic, irreversible degradation of **creatine** and **creatine phosphate**, primarily in muscles. - **Creatine** itself is synthesized endogenously from three amino acids: **glycine, arginine, and methionine** (as S-adenosylmethionine) through a two-step enzymatic process in the kidney and liver. - The amount of creatinine produced daily is relatively constant and directly proportional to an individual's **muscle mass**, making it a useful marker for renal function. *Lysine* - **Lysine** is an **essential amino acid** and a precursor for various compounds like **carnitine** but is not involved in creatinine or creatine formation. - Deficiency can lead to impaired protein synthesis but does not impact creatinine levels. *Leucine* - **Leucine** is another **essential amino acid** and a **branched-chain amino acid (BCAA)** crucial for muscle protein synthesis and repair. - It does not serve as a direct precursor for creatinine or creatine. *Histidine* - **Histidine** is an **essential amino acid** and a precursor for **histamine** and other important compounds, but not creatinine or creatine. - It plays roles in immune response and gastric acid secretion.

Q: What is the composition of epithelial sodium channels?

1α, 1β, 1γ. ***1α, 1β, 1γ*** - Epithelial sodium channels (**ENaCs**) are heterotrimeric complexes composed of one **alpha (α)**, one **beta (β)**, and one **gamma (γ) subunit**. - This specific subunit composition is essential for the channel's proper function in **sodium reabsorption** across epithelial tissues. *2α, 1β* - This composition is incomplete as it lacks the **gamma (γ) subunit**, which is a crucial component of the functional ENaC. - While alpha and beta subunits are present, the absence of the gamma subunit would impair the channel's ability to efficiently transport sodium. *2α, 1β, 2γ* - This composition is incorrect because a functional ENaC typically includes only **one gamma (γ) subunit**, not two. - An imbalance in subunit stoichiometry can lead to misfolding or improper assembly, affecting channel function. *2α, 1β, 1γ* - This combination correctly includes all three types of subunits (alpha, beta, gamma) but incorrectly states there are **two alpha (α) subunits**. - A functional ENaC has a single alpha subunit, making this option incorrect.

Q: Increase in plasma viscosity is maximally caused by which plasma protein?

Fibrinogen. ***Globulin*** - Increased levels of **globulin** proteins, particularly in inflammatory or proliferative conditions, have a significant impact on plasma viscosity due to their **high molecular weight** [1]. - **Globulins** contribute to **hyperviscosity syndrome**, which can lead to clinical symptoms like fatigue and visual disturbances [1]. *Albumin* - While **albumin** is the most abundant plasma protein, its primary role is in maintaining **oncotic pressure**, not significantly affecting plasma viscosity. - An increase in albumin does not correlate with plasma viscosity increases to the extent seen with globulins. *All have equal effect* - Different plasma proteins do not have **equal effects** on viscosity; **globulins** and **fibrinogen** particularly influence it more than **albumin**. - The impact on viscosity varies significantly with protein concentration and type, making this statement inaccurate. *Fibrinogen* - **Fibrinogen** does contribute to plasma viscosity but is typically less than that caused by globulins, especially when globulin levels are markedly elevated. - Its effect is more pronounced during **coagulation**, rather than in the general increase of plasma viscosity associated with inflammatory states. **References:** [1] Cross SS. Underwood's Pathology: A Clinical Approach. 6th ed. (Basic Pathology) introduces the student to key general principles of pathology, both as a medical science and as a clinical activity with a vital role in patient care. Part 2 (Disease Mechanisms) provides fundamental knowledge about the cellular and molecular processes involved in diseases, providing the rationale for their treatment. Part 3 (Systematic Pathology) deals in detail with specific diseases, with emphasis on the clinically important aspects., pp. 141-142.

Question 1

Which of the following statements is true regarding the functions of cAMP and cGMP?

Accepted Answer

They are both second messengers.

Answer

All of the above statements are true

Answer

They act on membrane receptors.

Answer

They act by post-translational modification.

Question 2

Which of the following compounds is not formed with the involvement of glycine?

Accepted Answer

Thyroxine

Answer

Purines

Answer

Glutathione

Answer

Heme

Question 3

Abnormal proteins which are bound to ubiquitin are degraded in -

Accepted Answer

Proteasomes

Answer

Golgi apparatus

Answer

Smooth ER

Answer

Lysosomes

Question 4

Coenzyme for phenylalanine hydroxylase is?

Accepted Answer

Tetrahydrobiopterin

Answer

Tetrahydrofolate

Answer

Pyridoxal phosphate

Answer

S-adenosyl methionine

Question 5

GlcNAc-P-P-oligosaccharide is -

Accepted Answer

Glycoprotein

Answer

Proteoglycan

Answer

Collagen

Answer

Phospholipid

Question 6

Prolyl hydroxylase requires which cofactor?

Accepted Answer

Vitamin C

Answer

Iron (Fe²⁺)

Answer

Molybdenum

Answer

Vitamin K1

Question 7

What type of bond is involved in the side chain linkage of proteoglycans?

Accepted Answer

Covalent

Answer

Hydrogen bond

Answer

Electrostatic bond

Answer

Van-der Waal's force

Question 8

Creatinine is formed from -

Accepted Answer

Creatine

Answer

Lysine

Answer

Leucine

Answer

Histidine

Question 9

What is the composition of epithelial sodium channels?

Accepted Answer

1α, 1β, 1γ

Answer

2α, 1β, 1γ

Answer

2α, 1β

Answer

2α, 1β, 2γ

Question 10

Increase in plasma viscosity is maximally caused by which plasma protein?

Accepted Answer

Fibrinogen

Answer

Albumin

Answer

All have equal effect

Answer

Globulin

NEET-PG 2015

Biochemistry

Physiology