MCQs

Linoleic acid (omega-6) and α-linolenic acid (omega-3) are essential fatty acids. Humans and other mammals lack the enzymes (Δ12 and Δ15 desaturases) to insert double bonds at the required positions in the fatty acid chain. They must be ingested in the diet to maintain health.

A phospholipid is a substituted triglyceride. Lecithin (phosphatidylcholine) consists of glycerol esterified to two fatty acids and a phosphate group, which is in turn esterified to the nitrogenous alcohol choline. Complete hydrolysis breaks all these ester bonds.

Active transport is the movement of molecules against a concentration gradient. This process is directly coupled to ATP hydrolysis as an energy source, for example, by the Na⁺/K⁺ pump. Passive processes like diffusion and facilitated diffusion are driven by the gradient itself and do not require ATP directly.

While all levels contribute, the precise 3D shape of an antigen-binding pocket is a feature of the protein's tertiary structure. It is formed by the folding and precise juxtaposition of R-groups from different parts of a single polypeptide chain (in heavy and light chains).

Uracil is a pyrimidine base found in RNA. Like thymine (its counterpart in DNA), its structure is complementary to adenine, and it forms two hydrogen bonds with adenine during base pairing. Guanine pairs with cytosine.

Secondary structures are defined by the pattern of hydrogen bonds between the carbonyl oxygen (C=O) and the amide hydrogen (N-H) of the peptide backbone itself. The R-groups are not involved; their interactions define the higher-level tertiary structure.

Zymogens like pepsinogen, trypsinogen, and chymotrypsinogen are inactive precursors of powerful proteases. They are activated by cleavage only after reaching the gut lumen. This prevents them from hydrolyzing the proteins of the cells that produce them, which would lead to tissue destruction.

The active site catalytic residues often depend on specific ionization states to function. At the optimum pH, these residues have the correct charge (+ or -) for substrate binding or catalysis. Deviation from this pH alters the ionization, disrupting the interactions and decreasing activity.

Glycogen is more extensively branched than starch's amylopectin. Branching creates numerous terminal non-reducing ends. Glycogen phosphorylase can act on all these ends simultaneously, leading to a much faster release of glucose-1-phosphate to fuel the animal's high metabolic rate.

The alternating single and double bonds (conjugation) in carotenoids create a delocalized electron system that can absorb specific wavelengths of visible light. This makes them colored pigments (e.g., orange in carrots, red in tomatoes) that play roles in photosynthesis and photoprotection.

A nucleoside consists of a nitrogenous base plus a pentose sugar. A nucleotide is a nucleoside with one or more phosphate groups covalently bonded to the 5' carbon (or 3' carbon) of the sugar. The addition of phosphate is the defining difference.

"Amphipathic" describes a molecule with both hydrophilic (water-loving, polar head group) and hydrophobic (water-fearing, non-polar fatty acid tails) parts. This dual property forces them into a bilayer arrangement where the heads face water and the tails are sequestered away from it.

The classification depends on the carbonyl group's position. If the carbonyl is at the end of the carbon chain (C1), it is an aldehyde group and the sugar is an aldose. If the carbonyl is on an inner carbon (C2 for the most common ketose, fructose), it is a ketone group and the sugar is a ketose.

A glycosidic bond is the covalent linkage that joins monosaccharides into polysaccharides. A peptide bond is the analogous covalent linkage that joins amino acids into polypeptide chains. Both are formed by dehydration synthesis and create the primary polymer backbone.

Some proteins can refold spontaneously into their native, biologically active conformation after the denaturing agent is gently removed. This is called renaturation. This ability indicates that the primary sequence remains intact and contains all the information for folding.

Aspirin (acetylsalicylic acid) acts by transferring its acetyl group to a serine hydroxyl in the active site of COX enzymes. This chemical modification is covalent and permanent (for the life of the enzyme), making it an irreversible inhibition, not a reversible binding interaction.

The cis-double bond introduces a fixed bend in the hydrocarbon tail. This prevents the fatty acid chains from packing closely together, increasing the free volume within the bilayer and thereby increasing its fluidity and permeability compared to saturated chains.

The amino acid is covalently attached to the 3' acceptor stem of its cognate tRNA molecule. During elongation, the peptidyl transferase center of the ribosome catalyzes the nucleophilic attack of the amino group of the incoming aminoacyl-tRNA on the ester bond of the peptidyl-tRNA.

Adipose tissue, rich in triglycerides, serves as a padding that protects vital organs from physical shock. It also functions as a thermal insulator in subdermal layers, reducing heat loss from the body. Energy storage is its primary role, but the options highlight these secondary roles.