By Fatskills Exam Guides Team — the exam nerds behind 28,500+ quizzes and 2.1M practice questions across 500+ global exams.
Q: What is a monomer? A: A small, repeating subunit that bonds to form polymers (e.g., glucose for starch, amino acids for proteins). Trap/Clarification: Monomers-functional units; polymers (e.g., enzymes) perform biological roles.
Q: What is a glycosidic linkage? A: A covalent bond between monosaccharides (e.g., glucose + fructose = sucrose) formed via dehydration synthesis. Trap/Clarification: Not all carbs have the same linkage (e.g., ?-1,4 in starch vs. ?-1,4 in cellulose).
Q: What is denaturation? A: Loss of a protein’s 3D shape (and function) due to heat, pH, or salinity disrupting hydrogen/ionic bonds. Trap/Clarification: Primary structure (peptide bonds) remains intact; only secondary/tertiary/quaternary levels unfold.
Q: Why are phospholipids amphipathic? A: Their hydrophilic phosphate heads and hydrophobic fatty acid tails enable spontaneous bilayer formation in aqueous environments (cell membranes). Trap/Clarification: Amphipathic-soluble; phospholipids form micelles/bilayers, not true solutions.
Q: Why is cellulose indigestible by humans? A: Humans lack cellulase enzymes to break ?-1,4 glycosidic bonds in cellulose; cows use gut microbes for this. Trap/Clarification: Cellulose is a carb, but its structure (linear, H-bonded fibers) makes it indigestible, not its composition.
Q: Why do unsaturated fats stay liquid at room temperature? A: Kinked fatty acid tails (from C=C double bonds) prevent tight packing, reducing van der Waals forces. Trap/Clarification: "Unsaturated" refers to double bonds, not fewer hydrogens (though that’s a consequence).
Q: How do you identify a reducing sugar? A: Use Benedict’s reagent (blue-red precipitate) if the sugar has a free aldehyde/ketone group (e.g., glucose, fructose; not sucrose). Trap/Clarification: Sucrose is non-reducing because its glycosidic bond locks both anomeric carbons.
Q: How is protein primary structure determined? A: Amino acid sequence is encoded by DNA-transcribed to mRNA-translated by ribosomes (peptide bonds form between amino/carboxyl groups). Trap/Clarification: Primary structure-3D shape; it’s just the linear sequence.
Q: How do you calculate the number of peptide bonds in a protein? A: # peptide bonds = # amino acids – 1 (e.g., 100 amino acids = 99 bonds). Trap/Clarification: Count bonds, not amino acids; the first amino acid has a free amino group.
Q: Can lipids dissolve in water? A: No; lipids are nonpolar/hydrophobic, but phospholipids can form emulsions (e.g., micelles) in water. Trap/Clarification: "Dissolve"-"form structures"; lipids don’t dissolve but can self-assemble.
Q: Under what conditions does a protein refold after denaturation? A: Only if the primary structure is intact and conditions (pH, temperature) return to optimal; chaperonins may assist. Trap/Clarification: Not all proteins refold; some aggregate irreversibly (e.g., cooked egg whites).
Statement: All proteins have quaternary structure. Answer: FALSE Why the common mistake happens: Students confuse potential for requirement; only multi-subunit proteins (e.g., hemoglobin) have quaternary structure.
Statement: Starch and glycogen are both ?-glucose polymers, but glycogen is more branched. Answer: TRUE Why the common mistake happens: Students assume all glucose polymers are identical; branching affects solubility and energy release speed.
Statement: A triglyceride with 3 unsaturated fatty acids is called a "polyunsaturated fat." Answer: FALSE Why the common mistake happens: "Polyunsaturated" refers to multiple double bonds in one fatty acid, not the number of unsaturated fatty acids in a triglyceride.
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