NEET-PG 2015 - Biochemistry Practice Questions

Q: The mechanism of action of uncouplers of oxidative phosphorylation involves:

Disruption of proton gradient across the inner membrane. ***Disruption of proton gradient across the inner membrane*** - Uncouplers such as **2,4-dinitrophenol** increase the permeability of the **inner mitochondrial membrane** to protons. - This dissipates the **proton motive force** that is normally used by ATP synthase to produce ATP, leading to the uncoupling of electron transport from ATP synthesis. *Inhibition of ATP synthase* - Inhibitors of ATP synthase directly block the enzyme's activity, preventing the synthesis of ATP while the **proton gradient** remains intact. - This mechanism is distinct from uncouplers, which allow electron transport to continue while dissipating the proton gradient. *Stimulation of ATP synthase* - Uncouplers do not stimulate ATP synthase; rather, their action prevents ATP synthase from effectively utilizing the **proton gradient** for ATP production. - Stimulation of ATP synthase would lead to increased ATP synthesis, which is contrary to the effect of uncouplers. *Blocking electron transport chain complexes* - Inhibitors of the **electron transport chain** (e.g., cyanide, rotenone) directly prevent the flow of electrons, thereby preventing the pumping of protons and the formation of a **proton gradient**. - Uncouplers, in contrast, allow electron transport to proceed but dissipate the proton gradient after it has been established.

Q: Converging point of both pathways in coagulation is at:

Stuart factor X. ***Stuart factor X*** [1][2] - It is the main **converging point** of the coagulation cascade, where both the intrinsic and extrinsic pathways meet to initiate the common pathway [1]. - Activated factor X leads to the conversion of **prothrombin to thrombin**, pivotal for clot formation [2]. *Factor VII* [2] - Primarily involved in the **extrinsic pathway** of coagulation, activating factor X, but does not serve as a converging point. - Its function is limited to starting the coagulation cascade, particularly upon tissue injury. *Factor IX* [2] - A key component of the **intrinsic pathway**, it leads to the activation of factor X but is not the point where both pathways converge. - It requires **factor VIII** for its activation, further illustrating its role within a specific pathway. *Factor VIII* - Also part of the **intrinsic pathway**, it acts as a cofactor for factor IX but does not integrate both pathways into a common point. - Its deficiency is associated with **Hemophilia A**, underscoring its specific pathway involvement. **References:** [1] Kumar V, Abbas AK, et al.. Robbins and Cotran Pathologic Basis of Disease. 9th ed. Hemodynamic Disorders, Thromboembolic Disease, and Shock, pp. 128-130. [2] Cross SS. Underwood's Pathology: A Clinical Approach. 6th ed. Common Clinical Problems From Blood And Bone Marrow Disease, pp. 582-583.

Q: Which protein does the domain of plasminogen resemble?

Apolipoprotein (a) (a lipoprotein). ***Apolipoprotein (a) (a lipoprotein)*** - **Plasminogen** and **apolipoprotein (a)** share structural homology, specifically due to the presence of **kringle domains**. - This structural similarity suggests a potential for apolipoprotein (a) to **interfere with plasminogen’s fibrinolytic activity**, contributing to **atherosclerosis**. *Fibrinogen (a clotting protein)* - While plasmin acts on fibrinogen (and its derivative fibrin), its domain structure does not **resemble fibrinogen**. - **Fibrinogen** is a large, multi-domain glycoprotein crucial for **clot formation**, distinct from plasminogen's primarily **kringle-rich structure**. *LDL receptor (a lipid metabolism protein)* - The **LDL receptor** is involved in **cholesterol uptake** by cells and has structural features like ligand-binding repeats and epidermal growth factor (EGF) repeats. - Its domain structure is **not similar to plasminogen**, which is characterized by **kringle domains** and a protease domain. *Prothrombin (a coagulation protein)* - **Prothrombin** is a precursor to thrombin, featuring **gla domains**, kringle-like domains (though structurally distinct from plasminogen's), and a serine protease domain. - While both are involved in coagulation/fibrinolysis, their **overall domain arrangements and specific kringle structures differ** significantly.

Q: Which of the following stimulates Acetyl CoA Carboxylase?

Citrate. ***Citrate*** - **Citrate** is an allosteric activator of **Acetyl-CoA Carboxylase (ACC)**, indicating abundant energy and precursor availability for fatty acid synthesis. - This activation promotes the conversion of **Acetyl-CoA** to **Malonyl-CoA**, the committed step in **fatty acid synthesis**. *Starvation* - **Starvation** leads to energy deficit, which generally **inhibits** anabolic processes like fatty acid synthesis. - In this state, enzymes involved in anabolic pathways are often downregulated or inhibited to conserve energy. *Glucagon* - **Glucagon** is a hormone that signals low blood glucose and promotes catabolic processes such as **glycogenolysis** and **gluconeogenesis**. - It **inhibits** fatty acid synthesis by phosphorylating and inactivating **Acetyl-CoA Carboxylase**, thus opposing citrate's activating effect. *None of the options* - **Citrate** is a known stimulator of Acetyl CoA Carboxylase. - This option is incorrect because there is a correct answer among the choices.

Q: What is the role of colipase in fat digestion?

Assists pancreatic lipase in fat digestion. ***Assists pancreatic lipase in fat digestion*** - Colipase **binds to pancreatic lipase** and the **lipid-water interface** of the fat droplet, providing a conformational change that enables lipase to access and hydrolyze triglycerides. - It also prevents bile salts from inactivating pancreatic lipase, ensuring efficient **fat emulsification and digestion**. *Is secreted in an inactive form* - Colipase is secreted as **procolipase** by the pancreas, which is then activated by **trypsin** in the duodenum. - While correct, this option describes its activation rather than its primary role in fat digestion. *Encoded by the gene CLPS* - The gene **CLPS** indeed encodes for colipase, but this is a genetic detail rather than its functional role in the digestive process. - Knowledge of the encoding gene is not directly relevant to understanding its biochemical function in fat digestion. *Is secreted by pancreatic cells* - Colipase is indeed synthesized and secreted by the **pancreas** into the small intestine. - This statement is true but describes the **origin** of colipase, not its specific functional role in fat digestion.

Q: Chymotrypsinogen is activated into chymotrypsin by:

Trypsin. ***Activation of Chymotrypsinogen by Trypsin*** - **Trypsin** is the primary enzyme responsible for the activation of **chymotrypsinogen** into its active form, **chymotrypsin**, by cleaving a specific peptide bond. - This activation is part of a cascade of proteolytic enzyme activations in the **pancreatic juice**, crucial for protein digestion in the small intestine. *Pepsin* - **Pepsin** is a protease active in the **stomach**, requiring an acidic environment for its activity, and is involved in the initial breakdown of proteins. - It does not play a role in the activation of pancreatic zymogens like chymotrypsinogen; its primary function is protein digestion in the gastric lumen. *Renin* - **Renin** is an enzyme primarily involved in the **renin-angiotensin-aldosterone system** (RAAS), which regulates blood pressure and fluid balance. - Its action involves cleaving **angiotensinogen** to form angiotensin I, and it has no role in the activation of digestive enzymes like chymotrypsinogen. *HCl* - **Hydrochloric acid (HCl)** is produced in the stomach and is essential for providing the acidic environment required for **pepsin's activity** and for denaturing proteins. - While HCl is crucial for digestion, it does not directly activate chymotrypsinogen; this activation is an enzymatic process carried out by another protease.

Q: HDL is called good cholesterol because -

Removes cholesterol from peripheral tissues. ***Removes cholesterol from peripheral tissues*** - **High-density lipoprotein (HDL)** is known as "good cholesterol" due to its role in **reverse cholesterol transport**, a process where it collects excess cholesterol from peripheral cells and tissues. - This action helps to prevent the accumulation of cholesterol in arteries, thereby reducing the risk of **atherosclerosis** and cardiovascular disease. - HDL then transports this cholesterol to the liver for excretion via bile, completing the protective cycle. *Increases cholesterol delivery to peripheral tissues* - This is actually the opposite of HDL's function and describes the role of **LDL (low-density lipoprotein)**, which is considered "bad cholesterol." - LDL delivers cholesterol to peripheral tissues, and excess LDL can lead to **atherosclerotic plaque formation**. *Stimulates cholesterol synthesis in the liver* - HDL does not directly stimulate cholesterol synthesis in the liver; rather, its role is primarily in **cholesterol efflux** from cells and transport. - The liver's cholesterol synthesis is regulated by various factors, including dietary intake and cellular cholesterol levels via the **SREBP pathway**, but HDL does not upregulate hepatic cholesterol synthesis. *Activates enzymes that break down triglycerides* - While HDL does activate **LCAT (lecithin-cholesterol acyltransferase)** for cholesterol esterification, its primary "good" function is not the breakdown of triglycerides. - **Lipoprotein lipase (LPL)** is the primary enzyme responsible for triglyceride breakdown in lipoproteins like VLDL and chylomicrons.

Q: Amide group is present in which part of protein?

Peptide bond. ***Peptide bond*** - A **peptide bond** is formed between the **carboxyl group** of one amino acid and the **amino group** of another, releasing a water molecule. This bond has an **amide structure**. - The repeated formation of these amide (peptide) bonds links amino acids into long chains, forming a **polypeptide** or protein. *Amino-terminal* - The **amino-terminal (N-terminal)** end of a protein contains a free **amino group (-NH2)**, which is not part of an amide linkage within the polypeptide backbone. - It marks the beginning of the polypeptide chain and is typically involved in various cellular interactions and modifications. *Disulfide bond* - A **disulfide bond** is a covalent bond formed between two **sulfhydryl groups (-SH)** of **cysteine residues**, leading to the formation of a **cystine** residue. - This bond is crucial for stabilizing the **tertiary and quaternary structures** of proteins, but it does not contain an amide group. *Carboxy-terminal* - The **carboxy-terminal (C-terminal)** end of a protein contains a free **carboxyl group (-COOH)**, which is not part of an amide linkage within the polypeptide backbone. - It marks the end of the polypeptide chain and plays roles in protein processing, targeting, and regulation.

Q: In phenylketonuria, which substance should be restricted in the diet?

Phenylalanine. ***Phenylalanine*** - **Phenylketonuria (PKU)** is a genetic disorder where the body cannot effectively metabolize **phenylalanine** due to a deficiency in the enzyme **phenylalanine hydroxylase**. - Restricting dietary phenylalanine is crucial to prevent the accumulation of toxic byproducts that can lead to severe neurological damage and developmental delays. *Tyrosine* - Tyrosine is normally synthesized from phenylalanine. In PKU, this conversion is impaired. - While phenylalanine must be restricted, tyrosine supplementation is often necessary for individuals with PKU, as it becomes a conditionally essential amino acid. *Maize* - Maize (corn) is a carbohydrate-rich food and does not contain high levels of phenylalanine that would necessitate its restriction in PKU. - Dietary management in PKU focuses on regulating protein intake, as phenylalanine is an amino acid found in proteins. *None of the options* - This option is incorrect because phenylalanine must be strictly restricted in the diet of individuals with phenylketonuria to manage the condition effectively. - Without dietary restriction, the accumulation of phenylalanine can lead to severe and irreversible neurological damage.

Q: Calcium absorption is hampered by

Phytates. ***Phytates*** - **Phytates** (phytic acid) found in whole grains, legumes, nuts, and seeds bind to calcium, forming an insoluble complex that significantly **reduces its absorption** in the intestines. - This binding prevents the free calcium ions from crossing the intestinal wall into the bloodstream. *Protein* - **Protein** generally *enhances* calcium absorption, especially when consumed in moderate amounts, as some amino acids can form soluble calcium complexes. - However, very high protein intake, particularly from animal sources, *may* slightly increase urinary calcium excretion in the long term, but it does not directly hamper intestinal absorption. *Lactose* - **Lactose**, a sugar found in milk, is known to *enhance* calcium absorption. - It does so by creating a more acidic environment in the small intestine and by forming soluble complexes with calcium, making it more bioavailable. *Acid* - **Stomach acid** (hydrochloric acid) is crucial for calcium absorption as it helps to solubilize calcium salts from food. - A *reduced* acidic environment, such as from antacid use or certain medical conditions, would hamper calcium absorption, but acid itself is beneficial.

Question 1

The mechanism of action of uncouplers of oxidative phosphorylation involves:

Accepted Answer

Disruption of proton gradient across the inner membrane

Answer

Inhibition of ATP synthase

Answer

Stimulation of ATP synthase

Answer

Blocking electron transport chain complexes

Question 2

Converging point of both pathways in coagulation is at:

Accepted Answer

Stuart factor X

Answer

Factor VIII

Answer

Factor IX

Answer

Factor VII

Question 3

Which protein does the domain of plasminogen resemble?

Accepted Answer

Apolipoprotein (a) (a lipoprotein)

Answer

Fibrinogen (a clotting protein)

Answer

LDL receptor (a lipid metabolism protein)

Answer

Prothrombin (a coagulation protein)

Question 4

Which of the following stimulates Acetyl CoA Carboxylase?

Accepted Answer

Citrate

Answer

Starvation

Answer

Glucagon

Answer

None of the options

Question 5

What is the role of colipase in fat digestion?

Accepted Answer

Assists pancreatic lipase in fat digestion

Answer

Encoded by the gene CLPS

Answer

Is secreted in an inactive form

Answer

Is secreted by pancreatic cells

Question 6

Chymotrypsinogen is activated into chymotrypsin by:

Accepted Answer

Trypsin

Answer

Pepsin

Answer

Renin

Answer

HCl

Question 7

HDL is called good cholesterol because -

Accepted Answer

Removes cholesterol from peripheral tissues

Answer

Increases cholesterol delivery to peripheral tissues

Answer

Stimulates cholesterol synthesis in the liver

Answer

Activates enzymes that break down triglycerides

Question 8

Amide group is present in which part of protein?

Accepted Answer

Peptide bond

Answer

Amino-terminal

Answer

Disulfide bond

Answer

Carboxy-terminal

Question 9

In phenylketonuria, which substance should be restricted in the diet?

Accepted Answer

Phenylalanine

Answer

Tyrosine

Answer

Maize

Answer

None of the options

Question 10

Calcium absorption is hampered by

Accepted Answer

Phytates

Answer

Protein

Answer

Lactose

Answer

Acid

NEET-PG 2015 — Biochemistry