Biomolecules & Macromolecules – Lecture Review

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A comprehensive set of Q&A flashcards covering key definitions, structures, functions, and examples of carbohydrates, lipids, proteins, and nucleic acids as outlined in the lecture notes.

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81 Terms

1
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What defines a macromolecule?

A very large molecule composed of thousands of covalently connected atoms.

2
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Which three classes of life’s organic molecules are true polymers?

Carbohydrates, proteins, and nucleic acids.

3
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What is a polymer?

A long molecule consisting of many similar or identical building blocks called monomers.

4
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Name the reaction that links monomers together in polymers.

Dehydration (condensation) reaction.

5
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What reaction breaks polymers into monomers?

Hydrolysis.

6
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Why are lipids not considered polymers?

Because they are not built from repeating monomeric sub-units in a long chain.

7
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What two factors determine the structure and function of a polysaccharide?

Its sugar monomers and the positions of glycosidic linkages.

8
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Give the general molecular formula for a monosaccharide.

A multiple of CH₂O (e.g., glucose = C₆H₁₂O₆).

9
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Which monosaccharide is most common in biology?

Glucose.

10
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How are monosaccharides classified?

By the position of the carbonyl group (aldose vs ketose) and the number of carbons in the skeleton.

11
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List the common triose, pentose, and hexose examples given in class.

Triose: glyceraldehyde; Pentose: ribose; Hexoses: glucose, galactose, fructose.

12
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In solution, monosaccharides form what structural shape?

Ring structures.

13
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What covalent bond joins two monosaccharides?

A glycosidic bond.

14
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Match each disaccharide to its monosaccharide components: lactose, maltose, sucrose.

Lactose = glucose + galactose; Maltose = glucose + glucose; Sucrose = glucose + fructose.

15
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What is the storage polysaccharide in plants?

Starch.

16
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Name the two structural forms of starch.

Amylose (unbranched) and amylopectin (branched).

17
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Where do plants store starch?

As granules inside chloroplasts and other plastids.

18
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What is the storage polysaccharide in animals?

Glycogen.

19
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In which tissues is glycogen primarily stored?

Liver and muscle cells.

20
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What structural polysaccharide forms plant cell walls?

Cellulose.

21
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What type of glucose linkage distinguishes cellulose from starch?

β-1,4 glycosidic linkages (cellulose) versus α-1,4 linkages (starch).

22
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Why can most animals digest starch but not cellulose?

Their enzymes hydrolyze α linkages in starch but cannot break β linkages in cellulose.

23
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What passes through the human gut as insoluble fiber?

Cellulose.

24
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Name the structural polysaccharide in arthropod exoskeletons and fungal cell walls.

Chitin.

25
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What unique functional group does chitin contain?

A nitrogen-containing amide group (N-acetylglucosamine).

26
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What two smaller molecules construct fats?

Glycerol and fatty acids.

27
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Define triacylglycerol (triglyceride).

A fat molecule consisting of glycerol linked to three fatty acids via ester linkages.

28
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Why are lipids hydrophobic?

They consist mostly of non-polar hydrocarbon chains that do not mix with water.

29
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Differentiate saturated and unsaturated fatty acids.

Saturated: no double bonds, straight chains, solid at room temperature; Unsaturated: one or more C=C double bonds, bent chains, liquid oils.

30
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What health risk is associated with a diet high in saturated fat?

Increased risk of cardiovascular disease due to plaque formation.

31
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Describe a phospholipid’s basic structure.

Two fatty acid tails and a phosphate-containing hydrophilic head attached to glycerol.

32
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What happens when phospholipids are placed in water?

They self-assemble into a bilayer with hydrophobic tails inward, forming the basis of cell membranes.

33
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What defines a steroid?

A lipid with a carbon skeleton of four fused rings.

34
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Why is cholesterol biologically important?

It stabilizes animal cell membranes and serves as a precursor for steroid hormones.

35
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List at least three major functions of proteins.

Enzymatic catalysis, structural support, storage, transport, cellular communication, movement, and defense.

36
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What monomers make up proteins?

Amino acids.

37
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How many different amino acids are used in proteins?

Twenty.

38
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Which part of an amino acid differs among the 20 varieties?

The R group (side chain).

39
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Identify the three categories of amino acid side chains.

Non-polar (hydrophobic), polar uncharged (hydrophilic), and electrically charged (acidic or basic).

40
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What type of bond links amino acids in a polypeptide?

Peptide bond.

41
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What are the N-terminus and C-terminus of a polypeptide?

The free amino (N) end and the free carboxyl (C) end, respectively.

42
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Name and briefly describe the four levels of protein structure.

Primary: amino acid sequence; Secondary: α-helix or β-sheet H-bonding patterns; Tertiary: 3-D folding via side-chain interactions; Quaternary: association of multiple polypeptides.

43
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Give one example each of proteins with quaternary structure.

Collagen (three polypeptides) and hemoglobin (two α + two β chains).

44
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How does a single amino acid substitution cause sickle-cell disease?

It alters hemoglobin’s primary structure, leading to abnormal aggregation and sickled red blood cells.

45
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Define protein denaturation.

The loss of a protein’s native conformation (and function) due to environmental changes such as pH, salt, or temperature.

46
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What are chaperonins?

Protein complexes that assist the proper folding of other proteins.

47
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Name two techniques used to determine protein 3-D structure.

X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy.

48
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What is a gene?

A unit of inheritance that encodes the amino acid sequence of a polypeptide, composed of DNA.

49
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List the three main types of RNA involved in protein synthesis.

Messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA).

50
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What are the monomers of nucleic acids called?

Nucleotides.

51
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Name the three components of a nucleotide.

Nitrogenous base, pentose sugar, and phosphate group.

52
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What is a nucleoside?

A nitrogenous base plus a sugar, without the phosphate.

53
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Differentiate purines and pyrimidines.

Purines (adenine, guanine) have a double ring; pyrimidines (cytosine, thymine, uracil) have a single six-membered ring.

54
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Which sugar is found in DNA and which in RNA?

DNA contains deoxyribose; RNA contains ribose.

55
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What covalent bond links nucleotides in a polynucleotide chain?

A phosphodiester bond between the 3′ hydroxyl of one nucleotide and the 5′ phosphate of the next.

56
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Describe the orientation of the two strands in the DNA double helix.

Antiparallel: one strand runs 5′→3′, the other 3′→5′.

57
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State the complementary base-pairing rules in DNA.

A pairs with T, and G pairs with C via hydrogen bonds.

58
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Why is complementary base pairing essential for DNA function?

It enables accurate replication and transcription, preserving genetic information.

59
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List three key differences between DNA and RNA.

DNA: deoxyribose sugar, thymine, double-stranded; RNA: ribose sugar, uracil, usually single-stranded.

60
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Explain the main implication of antiparallel strands for DNA replication.

DNA polymerases can only add nucleotides to the 3′ end, leading to leading and lagging strand synthesis.

61
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How can molecular biology be used to assess evolutionary relationships?

By comparing DNA or protein sequences; closer similarity indicates closer evolutionary kinship.

62
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What is the major biological role of fats?

Long-term energy storage.

63
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Which type of molecule forms microfibrils that strengthen plant cell walls?

Parallel β-glucose cellulose chains bound by hydrogen bonds.

64
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Why do phospholipid bilayers form spontaneously in aqueous environments?

Hydrophobic tails avoid water while hydrophilic heads interact with it, minimizing free energy.

65
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Which enzymes can hydrolyze α linkages but not β linkages?

Human digestive enzymes such as amylase for starch; they cannot digest cellulose.

66
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What structural feature of unsaturated fatty acids keeps plant oils liquid at room temperature?

Cis double bonds introduce kinks that prevent tight packing of molecules.

67
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Why does cholesterol at high blood levels pose a health risk?

It can contribute to plaque buildup in arteries, increasing cardiovascular disease risk.

68
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What is the role of hydrogen bonds in secondary protein structure?

They stabilize the α-helix and β-pleated sheet by linking backbone N–H and C=O groups.

69
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Give the one-letter code for the amino acid lysine.

K.

70
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Which amino acid contains a sulfhydryl (–SH) group capable of forming disulfide bridges?

Cysteine.

71
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During peptide bond formation, what molecule is released?

Water (H₂O).

72
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Explain why cellulose serves as dietary fiber for humans.

Humans lack enzymes to break β-1,4 linkages, so cellulose passes undigested, aiding bowel movement.

73
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What happens to a denatured protein if favourable conditions return?

Some proteins can renature and regain function; others cannot.

74
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Describe the basic flow of genetic information in cells (central dogma).

DNA → RNA → Protein.

75
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What is the major component of biological membranes?

A phospholipid bilayer.

76
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How do enzymes accelerate chemical reactions?

By lowering the activation energy barrier.

77
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Why are proteins said to be the most diverse macromolecules?

Because 20 amino acids in different sequences and conformations create an enormous range of structures and functions.

78
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What causes the sickle shape in red blood cells of affected individuals?

Aggregated mutant hemoglobin forms fibers that distort the cell.

79
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Name the bond that links glycerol to a fatty acid in fats.

Ester linkage.

80
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What is the defining chemical feature of a saturated fatty acid?

No carbon–carbon double bonds, fully saturated with hydrogen.

81
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Which macromolecule class includes hormones like insulin and glucagon?

Proteins (specifically, hormonal proteins).