brainscape_flashcards_topic1_full

(60 cards)

1
Q

What is a monomer?

A

A small molecule that can join with other molecules to form a polymer.

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2
Q

What is a polymer?

A

A large molecule made up of many monomers joined together.

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3
Q

What reaction forms polymers?

A

Condensation reaction - joins molecules and releases water.

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4
Q

What reaction breaks down polymers?

A

Hydrolysis reaction - breaks chemical bonds using water.

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5
Q

What is a monosaccharide?

A

A single sugar unit; monomer of carbohydrates.

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6
Q

Give three common monosaccharides.

A

Glucose, fructose, galactose.

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7
Q

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

A

OH on carbon 1 is below in α-glucose, above in β-glucose.

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8
Q

What is a disaccharide?

A

Two monosaccharides joined by a glycosidic bond in a condensation reaction.

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9
Q

Name three disaccharides and their components.

A
  • Maltose = glucose+glucose,
  • Sucrose = glucose+fructose,
  • Lactose = glucose+galactose.
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10
Q

What is a polysaccharide?

A

A carbohydrate made up of many monosaccharides joined by glycosidic bonds.

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11
Q

Describe the structure of starch.

A

Polysaccharide of α-glucose: amylose (unbranched), amylopectin (branched).

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12
Q

Why is starch a good storage molecule?

A

Compact, insoluble, and easily hydrolysed.

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13
Q

Describe the structure of glycogen.

A

Highly branched polymer of α-glucose.

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14
Q

Why is glycogen suited for energy storage in animals?

A

Highly branched for fast hydrolysis; compact and insoluble.

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15
Q

Describe the structure of cellulose.

A

Polymer of β-glucose with straight chains linked by hydrogen bonds into microfibrils.

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16
Q

Why is cellulose strong?

A

Many hydrogen bonds form strong microfibrils.

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17
Q

Describe the Benedict’s test for reducing sugars.

A

Add Benedict’s solution and heat; positive = red/orange/yellow/green precipitate.

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18
Q

How do you test for non-reducing sugars?

A

Hydrolyse with acid, neutralise, then redo Benedict’s test.

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19
Q

How do you test for starch?

A

Add iodine solution; positive = blue-black.

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20
Q

How can you estimate sugar concentration?

A

Use Benedict’s test, filter, dry and weigh precipitate or use a colorimeter.

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21
Q

How does a colorimeter help measure sugar concentration?

A

Measures absorbance of light through solution; use calibration curve to determine unknown.

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22
Q

What is a triglyceride?

A

A lipid made of 1 glycerol and 3 fatty acids.

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23
Q

What bond forms in triglycerides?

A

Ester bond.

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24
Q

What is the difference between saturated and unsaturated fatty acids?

A

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

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25
What is a phospholipid?
A lipid where one fatty acid is replaced by a phosphate group.
26
Why are phospholipids important in membranes?
Form bilayers; heads are hydrophilic, tails hydrophobic.
27
Describe the emulsion test for lipids.
Add ethanol, shake, add water; positive = milky white emulsion.
28
What is the general structure of an amino acid?
Amine group (NH2), carboxyl group (COOH), R group.
29
How do amino acids join?
Condensation reaction forming peptide bonds.
30
What is the primary structure of a protein?
The sequence of amino acids.
31
What is the secondary structure?
Folding into α-helix or β-pleated sheets via hydrogen bonds.
32
What is the tertiary structure?
3D folding due to R group interactions (H bonds, ionic bonds, disulfide bridges).
33
What is the quaternary structure?
Protein structure with more than one polypeptide chain.
34
Describe the Biuret test for proteins.
Add NaOH and CuSO4; positive = purple color.
35
How do enzymes speed up reactions?
Lower the activation energy.
36
Describe the induced fit model.
Substrate binding changes active site shape to fit more closely.
37
Why are enzymes specific?
Tertiary structure of active site is complementary to one substrate.
38
What affects enzyme activity?
Temperature, pH, substrate and enzyme concentration.
39
What happens to enzymes at high temperatures?
They denature; bonds break, active site changes.
40
What is a competitive inhibitor?
Molecule similar to substrate competes for active site.
41
What is a non-competitive inhibitor?
Binds to allosteric site, changing enzyme shape.
42
What variables affect enzyme reactions?
Temperature, pH, enzyme and substrate concentration, inhibitors.
43
How to measure rate of enzyme reaction?
Measure product/substrate change over time; rate = 1/time.
44
How to stop enzyme reactions?
Boil, add strong acid/alkali, use inhibitor.
45
Why use a colorimeter in enzyme experiments?
More accurate and objective than color matching.
46
What is DNA made of?
Two antiparallel strands of nucleotides with phosphodiester bonds.
47
What is RNA made of?
Single strand of nucleotides; ribose sugar; uracil instead of thymine.
48
How does DNA replicate?
Semi-conservative replication using DNA helicase and polymerase.
49
What enzyme forms phosphodiester bonds in DNA replication?
DNA polymerase.
50
What is ATP?
Adenosine triphosphate - energy currency of cells.
51
How is ATP broken down?
Hydrolysis by ATP hydrolase to ADP + Pi.
52
How is ATP made?
Condensation of ADP + Pi by ATP synthase during respiration/photosynthesis.
53
Why is ATP useful?
Releases small, manageable energy amounts quickly.
54
Why is water a good solvent?
It dissolves many polar substances.
55
Why is water important in temperature control?
High specific heat capacity buffers changes.
56
What makes water cohesive?
Hydrogen bonding between molecules.
57
Roles of hydrogen ions in biology?
Affect pH and enzyme activity.
58
Roles of iron ions?
Bind oxygen in haemoglobin.
59
Roles of sodium ions?
Co-transport of glucose/amino acids; nerve impulses.
60
Roles of phosphate ions?
Part of ATP, DNA, RNA, and phospholipids.