Protein Structure and Function — MCQs

Protein Structure and Function Indian Medical PG Practice Questions and MCQs

Question 451: Which of the following is the shortest peptide?

A. Oxytocin
B. Vasopressin
C. Angiotensin III (Correct Answer)
D. Angiotensin II

Explanation: ***Angiotensin III*** - **Angiotensin III** is a **heptapeptide**, meaning it consists of **7 amino acids**. - It is formed by the removal of the N-terminal aspartate from Angiotensin II (8 amino acids), making it the shortest peptide among the options. - It has similar but weaker actions compared to Angiotensin II in regulating blood pressure and aldosterone secretion. *Oxytocin* - **Oxytocin** is a **nonapeptide**, composed of **9 amino acids**. - It plays a role in uterine contractions during labor and milk ejection during lactation. *Vasopressin* - **Vasopressin**, also known as **antidiuretic hormone (ADH)**, is a **nonapeptide** (**9 amino acids**). - Its primary functions are water reabsorption in the kidneys and vasoconstriction. *Angiotensin II* - **Angiotensin II** is an **octapeptide**, containing **8 amino acids**. - It is a potent vasoconstrictor and stimulates aldosterone secretion, playing a key role in blood pressure regulation.

Question 452: Protein refolding is carried out by?

A. Valine
B. Threonine
C. Chaperone (Correct Answer)
D. Aspartate

Explanation: ***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.

Question 453: Which of the following is a ribozyme?

A. Peptidyl transferase (Correct Answer)
B. Elongation factor 2
C. Primase
D. RNA polymerase

Explanation: ***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.

Question 454: Which of the following types of bonds is considered the weakest?

A. Covalent
B. Hydrogen
C. Electrostatic
D. Van der Waals (Correct Answer)

Explanation: ***Van der Waals*** - **Van der Waals forces** are very **weak, short-range attractive forces** that arise from transient fluctuations in electron distribution, creating fleeting dipoles. - They are crucial for phenomena like **protein folding** and **molecular recognition**, but are easily overcome. *Covalent* - **Covalent bonds** involve the **sharing of electron pairs** between atoms, resulting in very strong and stable connections. - They require a significant amount of energy to break, making them fundamental to the structure of most organic and biological molecules. *Hydrogen* - **Hydrogen bonds** are **intermolecular forces** that occur when a hydrogen atom covalently bonded to a highly electronegative atom (like **oxygen** or **nitrogen**) is attracted to another electronegative atom. - While weaker than covalent bonds, they are significantly stronger than Van der Waals forces and play critical roles in **DNA structure** and **water properties**. *Electrostatic* - **Electrostatic interactions** (also known as **ionic bonds** or salt bridges) occur between oppositely charged ions or polar molecules. - These forces can be quite strong, especially in a non-polar environment, and are important for **protein stability** and **enzyme-substrate binding**.

Question 455: Which of the following is a tripeptide?

A. Glutathione (Correct Answer)
B. Angiotensin
C. Glucagon
D. Oxytocin

Explanation: ***Glutathione*** - **Glutathione** is a tripeptide composed of three amino acids: **glutamate**, **cysteine**, and **glycine**. - It plays a crucial role as an **antioxidant** in the body, protecting cells from damage by **free radicals**. *Angiotensin* - **Angiotensin** is a peptide hormone that causes **vasoconstriction** and an increase in **blood pressure**. - It is an **oligopeptide** (typically 8-10 amino acids) rather than a tripeptide. *Glucagon* - **Glucagon** is a peptide hormone produced by the **alpha cells** of the pancreas that raises **blood glucose levels**. - It is a **29-amino acid** polypeptide, much larger than a tripeptide. *Oxytocin* - **Oxytocin** is a hormone involved in social bonding and sexual reproduction, best known for its role in **childbirth** and **lactation**. - It is a **nonapeptide**, meaning it consists of nine amino acids.

Question 456: What is the primary amino acid responsible for the unique triple helix structure of collagen?

A. Glycine (Correct Answer)
B. Alanine
C. Arginine
D. Histidine

Explanation: ***Glycine*** - **Glycine** is the smallest amino acid, lacking a side chain (just a hydrogen atom), which allows for the tight packing required for the formation of collagen's **triple helix structure**. - It appears at every third position in the collagen polypeptide chain, often in the sequence **Gly-X-Y**, where X and Y are often **proline** and **hydroxyproline**. *Alanine* - **Alanine** has a methyl group side chain, which is larger than glycine's hydrogen atom, preventing the close packing necessary for the tight collagen helix. - While present in collagen, alanine does not occupy the critical every-third position responsible for the unique structural motif. *Arginine* - **Arginine** has a bulky and charged side chain, making it unsuitable for the interior of the tightly packed collagen triple helix. - Its presence would introduce steric hindrance and electrostatic repulsion, destabilizing the structure. *Histidine* - **Histidine** also possesses a relatively bulky and charged imidazole ring side chain, which would sterically hinder the tight coiling of the collagen strands. - It is not found in the high frequency or specific positions (Gly-X-Y) essential for forming the collagen triple helix.

Question 457: Which of the following statements about protein denaturation is correct?

A. Biological properties are retained after denaturation.
B. Denaturation is always irreversible.
C. The primary structure of the protein is unaffected. (Correct Answer)
D. Denaturation never results in proteins becoming insoluble.

Explanation: ***The primary structure of the protein is unaffected.*** - Denaturation refers to the disruption of a protein's **secondary, tertiary, and quaternary structures**, while the **covalent peptide bonds** that form the primary structure remain intact. - The sequence of amino acids, which defines the primary structure, is not typically altered by denaturing agents such as heat, pH changes, or chemicals. *Biological properties are retained after denaturation.* - Denaturation typically leads to the **loss of a protein's specific three-dimensional shape**, which is essential for its biological function. - Therefore, the biological properties and **activity of the protein are usually lost** or significantly impaired upon denaturation. *Denaturation is always irreversible.* - While many cases of denaturation are irreversible (e.g., cooking an egg), some proteins can **renature** if the denaturing conditions are removed, restoring their original structure and function. - This reversibility depends on the **severity and duration of the denaturing agent**, as well as the protein's inherent stability. *Denaturation never results in proteins becoming insoluble.* - Denaturation often exposes **hydrophobic regions** of a protein that were previously buried within its folded structure, leading to aggregation and **precipitation**, thereby making the protein insoluble. - This insolubility is a common consequence of denaturation, particularly with significant structural disruption.

Question 458: What is the primary metal ion found in myoglobin?

A. Iron (Correct Answer)
B. Copper
C. Selenium
D. Zinc

Explanation: ***Iron*** - **Iron** is the central metal ion in the **heme group** of myoglobin. - It is responsible for **binding oxygen** reversibly, which is myoglobin's primary function in muscle tissue. *Copper* - **Copper** is a component of several enzymes, such as **cytochrome c oxidase** and **superoxide dismutase**, but not myoglobin. - It plays a role in **electron transport** and connective tissue formation. *Selenium* - **Selenium** is an essential trace element that functions as a component of **glutathione peroxidase**, an antioxidant enzyme. - It is not found in the structure of myoglobin. *Zinc* - **Zinc** is a critical component of many enzymes, including **carbonic anhydrase** and **DNA polymerase**. - It is involved in **immune function** and wound healing, but not in oxygen transport by myoglobin.

Question 459: Which amino acid among the following has significant UV absorption at 280 nm used in protein quantification?

A. Tyrosine (Correct Answer)
B. Alanine
C. Histidine
D. Arginine

Explanation: ***Correct Option: Tyrosine*** - Tyrosine contains a **phenol functional group** (aromatic ring with hydroxyl group), giving it **significant UV absorption at 280 nm** (specifically ~274 nm) - Along with **tryptophan** and **phenylalanine**, tyrosine is one of the three aromatic amino acids used for **protein quantification via UV spectroscopy** - The aromatic side chain with conjugated double bonds enables strong UV light absorption *Incorrect Option: Alanine* - Alanine has a **methyl group** as its side chain (non-polar, aliphatic) - **Lacks aromatic rings** or conjugated systems - Does **not absorb UV light** at 280 nm *Incorrect Option: Histidine* - Histidine has an **imidazole ring** (heterocyclic aromatic) in its side chain - While technically aromatic, it has **minimal UV absorption at 280 nm** (weak absorption around 210-230 nm) - **Not used for protein quantification** at 280 nm due to insignificant absorption at this wavelength *Incorrect Option: Arginine* - Arginine contains a **guanidinium group** (highly basic, polar) - **Non-aromatic structure** without conjugated double bonds - Does **not exhibit UV absorption** at wavelengths used for protein analysis

Question 460: Protein glycosylation occurs in:

A. Peroxisomes
B. Endoplasmic reticulum (ER) (Correct Answer)
C. Mitochondria
D. Golgi bodies

Explanation: ***ER*** - **N-linked glycosylation**, the most common type of protein glycosylation, initiates in the **endoplasmic reticulum (ER)**, where an oligosaccharide precursor is transferred to asparagine residues of newly synthesized proteins. - The ER environment facilitates protein folding and quality control, ensuring correctly folded glycoproteins are transported further. *Golgi bodies* - While **further modification and processing** of glycosylated proteins occur in the Golgi apparatus, the initial step of N-linked glycosylation begins in the ER. - The Golgi is responsible for trimming and adding different sugar residues to complete the **glycan chains** and for sorting the glycoproteins to their final destinations. *Mitochondria* - Mitochondria are primarily involved in **cellular respiration** and **ATP production**. - They do not play a significant role in protein glycosylation; most mitochondrial proteins are imported from the cytoplasm in an unglycosylated state. *Peroxisomes* - Peroxisomes are involved in various **metabolic processes**, including fatty acid oxidation and detoxification. - They are not known to be sites of protein glycosylation.

Practice by Chapter

Amino Acids: Structure and Properties

Practice Questions

Peptide Bond Formation

Practice Questions

Primary Structure of Proteins

Practice Questions

Secondary Structure of Proteins

Practice Questions

Tertiary and Quaternary Structures

Practice Questions

Protein Folding and Chaperones

Practice Questions

Protein Domains and Motifs

Practice Questions

Structure-Function Relationships

Practice Questions

Hemoglobin and Myoglobin

Practice Questions

Collagen and Elastin

Practice Questions

Albumin and Plasma Proteins

Practice Questions

Post-Translational Modifications

Practice Questions

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