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Unit Won Flashcards

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1
Q

What are monomers?

A

Smaller / repeating molecules from which larger molecules / polymers are made.

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2
Q

What is a polymer?

A

Molecule made up of many identical / similar molecules / monomers.

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3
Q

What happens in a condensation reaction?

A

2 molecules join together, forming a chemical bond and releasing a water molecule.

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4
Q

What happens in a hydrolysis reaction?

A

2 molecules are separated by breaking a chemical bond and using a water molecule.

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5
Q

Give examples of common monomers and their corresponding polymers.

A

Monosaccharides: Glucose, fructose, galactose; Polymers: Starch, glycogen, cellulose.

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6
Q

What are monosaccharides?

A

Monomers from which larger carbohydrates are made.

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7
Q

List 3 common monosaccharides.

A
  • Glucose
  • Fructose
  • Galactose
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8
Q

What is the difference between α-glucose and β-glucose?

A

In α-glucose, the OH group is below carbon 1; in β-glucose, it is above carbon 1.

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9
Q

What are disaccharides?

A

Two monosaccharides joined together with a glycosidic bond, formed by a condensation reaction.

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10
Q

Name 3 common disaccharides and their monosaccharide components.

A
  • Maltose: Glucose + Glucose
  • Sucrose: Glucose + Fructose
  • Lactose: Glucose + Galactose
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11
Q

What are polysaccharides?

A

Many monosaccharides joined together with glycosidic bonds, formed by many condensation reactions.

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12
Q

Describe the structure and function of starch.

A

Polysaccharide of α-glucose; energy store in plant cells, with amylose (unbranched) and amylopectin (branched).

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13
Q

Describe the structure and function of glycogen.

A

Polysaccharide made of α-glucose; energy store in animal cells, branched structure.

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14
Q

Explain how the structure of starch relates to its function.

A

Helical structure is compact for storage; large, insoluble molecule does not affect water potential.

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15
Q

Explain how the structure of glycogen relates to its function.

A

Branched structure allows for compact storage and faster hydrolysis for glucose release.

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16
Q

What is cellulose?

A

Polysaccharide of β-glucose providing strength and structural support to plant / algal cell walls.

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17
Q

How does the structure of cellulose relate to its function?

A

Inverted β-glucose molecules form long, unbranched chains linked by hydrogen bonds, creating strong microfibrils.

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18
Q

Describe the test for reducing sugars.

A

Add Benedict’s solution, heat, and a positive result is green/yellow/orange/red precipitate.

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19
Q

Describe the test for non-reducing sugars.

A

First do Benedict’s test, then hydrolyze with acid, neutralize, and repeat Benedict’s test.

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20
Q

Describe the biochemical test for starch.

A

Add iodine dissolved in potassium iodide; positive result is blue-black.

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21
Q

Name two groups of lipids.

A
  • Triglycerides
  • Phospholipids
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22
Q

Describe the structure of a fatty acid.

A

Variable R-group (hydrocarbon chain) and a -COOH (carboxyl) group.

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23
Q

What distinguishes saturated fatty acids from unsaturated fatty acids?

A

Saturated: no C=C double bonds; Unsaturated: one or more C=C double bonds.

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24
Q

How do triglycerides form?

A

1 glycerol molecule and 3 fatty acids via condensation reactions forming 3 ester bonds.

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25
What property of triglycerides relates to their structure?
High ratio of C-H bonds means they release more energy than carbohydrates.
26
Describe the structure of phospholipids.
Similar to triglycerides but one fatty acid is replaced by a phosphate-containing group.
27
How do phospholipids function in cell membranes?
Form a bilayer allowing lipid-soluble substances to diffuse while restricting water-soluble substances.
28
Describe the test for lipids.
Add ethanol, shake, then add water; positive result is a milky white emulsion.
29
Describe the general structure of an amino acid.
COOH (carboxyl group), R (variable side chain), H2N (amine group).
30
How many amino acids are common in all organisms?
20 amino acids that differ only in their side group (R).
31
What is a dipeptide?
2 amino acids joined together.
32
What is a polypeptide?
Many amino acids joined together.
33
What is the primary structure of a protein?
Sequence of amino acids in a polypeptide chain, joined by peptide bonds.
34
What is the secondary structure of a protein?
Folding of the polypeptide chain into patterns like alpha helix or beta pleated sheets due to hydrogen bonding.
35
What is the tertiary structure of a protein?
3D folding of polypeptide chain due to interactions between amino acid R groups.
36
What is the quaternary structure of a protein?
More than one polypeptide chain formed by interactions between polypeptides.
37
Describe the test for proteins.
Add biuret reagent; positive result is purple/lilac color indicating presence of peptide bonds.
38
How do enzymes act as biological catalysts?
They lower activation energy of reactions to speed up the rate of reaction.
39
What is the induced-fit model of enzyme action?
Substrate binds to active site, causing a shape change to form enzyme-substrate complex.
40
What model of enzyme action was initially used?
Lock and key model.
41
What model describes the action of enzymes where the active site changes shape to fit the substrate?
Induced-fit model ## Footnote The induced-fit model contrasts with the lock and key model, where the active site is a fixed shape.
42
In the induced-fit model, what happens when the substrate binds to the enzyme?
Active site changes shape slightly to become complementary to the substrate
43
What is the initial model of enzyme action that is now considered outdated?
Lock and key model
44
What determines the specificity of enzymes?
Specific tertiary structure of the active site, dependent on amino acid sequence
45
As enzyme concentration increases, what happens to the rate of enzyme-controlled reactions?
Rate of reaction increases until substrate concentration becomes limiting
46
What is the limiting factor when enzyme concentration is high and substrate concentration is low?
Substrate concentration
47
How does increasing substrate concentration affect the rate of enzyme-controlled reactions?
Rate of reaction increases until enzyme concentration becomes limiting
48
What happens to the rate of reaction when temperature increases up to the optimum?
Rate of reaction increases due to more kinetic energy
49
What occurs to enzymes when the temperature exceeds the optimum?
Enzymes denature, causing the active site to change shape
50
How does pH affect enzyme activity?
Rate of reaction decreases as pH moves away from optimum due to denaturation
51
What is the effect of increasing concentration of competitive inhibitors on enzyme activity?
Rate of reaction decreases as inhibitors compete for the active site
52
Do non-competitive inhibitors affect the rate of reaction with increased substrate concentration?
No, they do not affect the rate as they bind to a different site
53
What is a common mistake regarding enzyme-substrate complexes?
Using the abbreviation 'E-S complexes' instead of the full term
54
What is the basic function of DNA?
Holds genetic information that codes for polypeptides
55
What is the primary function of RNA?
Transfers genetic information from DNA to ribosomes
56
What are the two types of molecules that make up a ribosome?
RNA and proteins
57
What distinguishes a DNA nucleotide from an RNA nucleotide?
DNA has deoxyribose sugar; RNA has ribose sugar
58
What type of bond forms between nucleotides in polynucleotides?
Phosphodiester bonds
59
What is the structure of DNA?
Polymer of nucleotides forming a double helix
60
What type of structure does messenger RNA have?
Single-stranded helix
61
What is the importance of semi-conservative replication?
Ensures genetic continuity between generations of cells
62
What enzyme breaks hydrogen bonds during DNA replication?
DNA helicase
63
What is the role of DNA polymerase during replication?
Joins adjacent nucleotides by forming phosphodiester bonds
64
Who proposed the models of the chemical structure of DNA?
Watson and Crick
65
What is ATP?
Adenosine triphosphate
66
Describe the structure of ATP.
Ribose bound to adenine and three phosphate groups
67
How is ATP broken down?
ATP is hydrolyzed to ADP and inorganic phosphate
68
Name two uses of ATP hydrolysis in cells.
* Coupled to energy-requiring reactions * Phosphorylation of other compounds
69
How is ATP resynthesized in cells?
ADP + Pi → ATP
70
What is the chemical formula for ATP?
Adenosine triphosphate (ATP) ## Footnote ATP consists of adenosine and three phosphate groups.
71
What type of reaction is ATP hydrolysis?
Hydrolysis reaction, using a water molecule ## Footnote This reaction is catalyzed by ATP hydrolase.
72
Name two ways in which the hydrolysis of ATP is used in cells.
* Coupled to energy requiring reactions within cells (releases / provides energy) * Inorganic phosphate released can be used to phosphorylate other compounds, making them more reactive
73
How is ATP resynthesized in cells?
ADP + Pi → ATP (+ water) ## Footnote This is a condensation reaction, catalyzed by ATP synthase.
74
During which processes is ATP resynthesized?
* Respiration * Photosynthesis
75
List properties of ATP that make it a suitable immediate source of energy for cells.
* Releases energy in relatively small amounts * Little energy lost as heat * Single reaction to release energy * Cannot pass out of cell
76
True or False: ATP can be stored within cells.
False ## Footnote ATP is too unstable to be stored.
77
What is water classified as, due to its molecular structure?
Polar molecule ## Footnote This polarity leads to hydrogen bonding.
78
Explain how hydrogen bonds occur between water molecules.
Slightly negatively charged oxygen atoms attract slightly positively charged hydrogen atoms of other water molecules.
79
List five properties of water that are important in biology.
* Metabolite * Solvent * High specific heat capacity * High latent heat of vaporisation * Strong cohesion between water molecules
80
What role does water play as a solvent in biological processes?
* Allows metabolic reactions to occur faster in solution * Allows transport of substances (e.g., nitrates in xylem, urea in blood)
81
What is the importance of water's high specific heat capacity in biology?
* Buffers changes in temperature * Provides a stable habitat for aquatic organisms * Helps organisms maintain a constant internal body temperature
82
What is the significance of water's high latent heat of vaporisation?
Allows effective cooling via evaporation of a small volume ## Footnote This helps organisms maintain a constant internal body temperature.
83
Describe the role of hydrogen ions (H+) in the body.
Maintain pH levels in the body; high concentration = acidic, which can affect enzyme activity.
84
What is the role of iron ions (Fe2+) in the body?
Component of haem group of haemoglobin, allowing oxygen transport as oxyhaemoglobin.
85
What are two roles of sodium ions (Na+) in the body?
* Involved in co-transport of glucose / amino acids into cells * Involved in action potentials in neurons
86
What is the role of phosphate ions (PO4^3-) in biological molecules?
* Component of nucleotides in DNA / RNA * Component of ATP * Phosphorylates other compounds * Hydrophilic part of phospholipids
87
True or False: Water is a solute.
False ## Footnote Water is a solvent that dissolves other substances (solutes).

Biology (8 decks)

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