Free Macromolecules MCQs with Answers

299 Macromolecules MCQs from Chemistry, each with the correct answer and a written explanation of why it is correct. Free and unlimited, with no account needed.

Proteins are classified by shape, composition and structure, from primary amino acid sequence to secondary, tertiary and quaternary organisation, and their biological roles are linked to this structure. Enzymes are examined as protein biocatalysts, including active sites, substrate specificity, activation energy, cofactors and factors affecting activity.

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299 questions · page 1 of 15

  • A. a glycosidic linkage
  • B. a peptide linkage, formed by condensation between a carboxyl and an amino group
  • C. an ester linkage
  • D. a hydrogen bond

Explanation: The carboxyl group of one amino acid condenses with the amino group of the next, releasing water and leaving a CO-NH amide link known as…

Correct answer: a peptide linkage, formed by condensation between a carboxyl and an amino group
  • A. dissolves only in organic solvents
  • B. contains a benzene ring
  • C. contains both an acidic carboxyl group and a basic amino group, so it reacts with both acids and bases
  • D. has no charge under any conditions

Explanation: The carboxyl group can donate a proton and the amino group can accept one, so an amino acid neutralises both acids and alkalis.

Correct answer: contains both an acidic carboxyl group and a basic amino group, so it reacts with both acids and bases
  • A. neutral point
  • B. isoelectric point
  • C. equivalence point
  • D. melting point

Explanation: At the isoelectric point the positive and negative charges within the molecule exactly balance, so the net charge is zero and the amino…

Correct answer: isoelectric point
Fairly easy
  • A. insoluble in water and structural in function
  • B. soluble in water and catalytic in function
  • C. always an enzyme
  • D. made of a single amino acid repeated

Explanation: Fibrous proteins consist of long parallel chains held in bundles, which makes them tough, insoluble and suited to structural roles in…

Correct answer: insoluble in water and structural in function
  • A. peptide bonds between amino acids
  • B. ionic bonds between side chains only
  • C. hydrogen bonds between the carbonyl and amide groups of the backbone
  • D. disulphide bridges only

Explanation: Regular coiling or pleating arises because each carbonyl oxygen hydrogen bonds to an amide hydrogen further along the same chain, giving…

Correct answer: hydrogen bonds between the carbonyl and amide groups of the backbone
Moderate
  • A. hydrolysis of all its peptide bonds
  • B. loss of its three dimensional shape while the amino acid sequence remains intact
  • C. a change in its amino acid sequence
  • D. conversion of the protein into a carbohydrate

Explanation: Heat, extreme pH, heavy metal ions and alcohol break the weak interactions holding the fold, so the chain unravels and biological activity…

Correct answer: loss of its three dimensional shape while the amino acid sequence remains intact
Fairly easy
  • A. glucose molecules
  • B. fatty acids and glycerol
  • C. a mixture of amino acids
  • D. urea and ammonia

Explanation: Every peptide bond is broken by boiling with concentrated acid or by protease enzymes, releasing the constituent amino acids, which can…

Correct answer: a mixture of amino acids
Moderate
  • A. Acting as enzymes
  • B. Transporting oxygen
  • C. Providing antibodies for defence
  • D. Serving as the main long term energy store

Explanation: The body stores energy as fat and, in the short term, as glycogen, and proteins are broken down for energy only when those stores are…

Correct answer: Serving as the main long term energy store
  • A. a violet colour with copper two ions in alkaline solution
  • B. a brick red precipitate
  • C. a silver mirror
  • D. a blue black colour

Explanation: Copper two ions form a violet complex with the peptide linkages, so the test detects the presence of peptide bonds rather than any…

Correct answer: a violet colour with copper two ions in alkaline solution
Moderate
  • A. are used up in the reactions they catalyse
  • B. raise the activation energy of a reaction
  • C. supply energy to drive unfavourable reactions
  • D. speed up reactions by lowering the activation energy and are recovered unchanged

Explanation: An enzyme provides an alternative pathway with a smaller energy barrier, so a far larger proportion of collisions are effective at body…

Correct answer: speed up reactions by lowering the activation energy and are recovered unchanged
Moderate
  • A. the shape and chemistry of its active site
  • B. its molar mass
  • C. the temperature of the reaction
  • D. the concentration of the substrate

Explanation: Only a substrate whose shape and charge distribution complement the active site can bind, which is why sucrase acts on sucrose but not on…

Correct answer: the shape and chemistry of its active site
Very hard
  • A. the substrate evaporates
  • B. the enzyme is denatured as the weak bonds holding its tertiary structure break
  • C. the enzyme is used up faster
  • D. the activation energy increases

Explanation: Heat disrupts the hydrogen and ionic interactions that hold the chain in shape, so the active site loses its precise geometry and can no…

Correct answer: the enzyme is denatured as the weak bonds holding its tertiary structure break
  • A. denaturing the enzyme permanently
  • B. binding an allosteric site
  • C. occupying the active site because it resembles the substrate
  • D. lowering the temperature

Explanation: Substrate and inhibitor compete for the same site, so the inhibition can be overcome by increasing the substrate concentration and the…

Correct answer: occupying the active site because it resembles the substrate
  • A. Protein and glucose
  • B. Starch and amino acid
  • C. Nucleic acid and fatty acid
  • D. Protein and amino acid

Explanation: Proteins are polymers of amino acids, starch and cellulose of glucose, and nucleic acids of nucleotides, while fats are not true polymers…

Correct answer: Protein and amino acid
  • A. contains a disulphide bridge
  • B. is fibrous
  • C. consists of two or more polypeptide chains associated together
  • D. contains more than one hundred amino acids

Explanation: Quaternary structure describes how separate polypeptide subunits fit together, as in haemoglobin with its two alpha and two beta chains…

Correct answer: consists of two or more polypeptide chains associated together
  • A. only amino acids
  • B. a non protein prosthetic group in addition to the polypeptide
  • C. no peptide bonds
  • D. two identical chains

Explanation: A conjugated protein is bound to a non protein group, so haemoglobin carries a haem group, glycoproteins carry carbohydrate and…

Correct answer: a non protein prosthetic group in addition to the polypeptide
  • A. increase enzyme activity uncontrollably
  • B. are converted into proteins by the body
  • C. supply too much energy to the cell
  • D. bind to sulphur containing groups in enzymes and denature them irreversibly

Explanation: These ions attack the sulphydryl side chains of cysteine, breaking disulphide bridges and destroying the tertiary structure, so the…

Correct answer: bind to sulphur containing groups in enzymes and denature them irreversibly
  • A. alters the charges on the side chains, changing the shape of the active site
  • B. changes the molar mass of the enzyme
  • C. removes the substrate from the solution
  • D. converts the enzyme into a carbohydrate

Explanation: Excess hydrogen or hydroxide ions interfere with the ionic and hydrogen bonds between side chains, distorting the active site so the…

Correct answer: alters the charges on the side chains, changing the shape of the active site
  • A. the fastest source of energy
  • B. amino acids for the growth and repair of tissues
  • C. essential fatty acids
  • D. dietary fibre

Explanation: Digested protein provides the amino acids the body reassembles into its own enzymes, hormones, antibodies and structural tissue, and this…

Correct answer: amino acids for the growth and repair of tissues
Fairly easy
  • A. the sequence of amino acids joined by peptide bonds
  • B. the coiling of the chain into a helix
  • C. the folding of the chain into a globular shape
  • D. the association of several chains

Explanation: Primary structure is simply the order of the residues, and it determines every higher level of structure, because the chain folds…

Correct answer: the sequence of amino acids joined by peptide bonds

Macromolecules MCQs: common questions

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