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Grade 12 Biology > Unit 1 > Flashcards

Unit 1 Flashcards

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1
Q

What are the biological atoms?

A

Sulfur, Phosphorus, Oxygen, Nitrogen, Carbon and Hydrogen

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2
Q

What is a macro-molecule?

A

a large complex structure

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3
Q

What is a polymer?

A

chain of repeating smaller subunits linked by covalent bonds

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4
Q

What are the 4 types of macro-molecules?

A

Proteins, Carbohydrates, Lipids, Nucleic Acids

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5
Q

What is a carbohydrate?

A

biological macromolecule that always has carbon, hydrogen and oxygen in a 1:2:1 ratio. Also has a high number of hydroxyl groups to allow for energy storage

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6
Q

What is starch used for?

A

short term energy storage in plants

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7
Q

What is glycogen used for?

A

short term energy in animals and an be broken down for energy faster than starch

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8
Q

What is cellulose used for?

A

provides structural support in plants

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9
Q

What is a lipid?

A

biological macromolecule with high proportions of non-polar CH bonds and they are hydrophobic whch plays a key role in determining their function

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10
Q

Why are lipids good for long term energy storage? Why not?

A

they have many CH bonds which can store energy longer but they are also less accessible so are used after carbohydrates.

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11
Q

How are lipids used in humans?

A

insulation, protection for major organs, in cell membranes

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12
Q

What are the main structural features of a carbohydrate?

A
  • lots of OH (hydroxyl) groups

- carbon, hydrogen and oxygen occur in 1:2:1 ratio

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13
Q

What are the main structural features of a lipid?

A
  • have long tails with many carbons
  • have ester bond and a double bonded oxygen
  • has a head and tail ends (usually)
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14
Q

What is a triglyceride?

A

lipid molecule made of glycerol molecule and 3 fatty acids linked by ester bonds

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15
Q

What is a fatty acid?

A

a hydrocarbon chain ending in a carboxyl group (COOH)

- can be saturated (all single bonds) or unsaturated (1+ double bonds)

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16
Q

What is monounsaturated?

A

one double bond

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17
Q

What is polyunstaurated?

A

2 or more double bonds. Humans cannot sythesize this so it is necessary in our diets.

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18
Q

What is a phospholipid?

A

composed of a glycerol molecule bonded to 2 fatty acids and a phosphate group with an R group.

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19
Q

What are phospholipids commonly found in?

A

they make up the cell membrane

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20
Q

What is so important about the head and the tail of a phospholipid?

A

the head is polar and hydrophillic and the tail is non-polar and hydrophobic. This is important in forming the phospholipid bilayer.

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21
Q

What is the phospholipid bilayer?

A

structure with heads of phospholipid toward aqueous envirronment in cells cytoplasm and extracellular fluid and tails toward centre interacting with each other

22
Q

What are some other lipids?

A

Cholesterol, Steroids, Waxes

23
Q

What is a protein?

A

has an amino group and carboxyl functional group and an R group that determines the amino acid

24
Q

What are the main structural features of a protein?

A
  • amino group (look for the nitrogen)
  • has an R group
  • has a carboxyl group (carbon with both a double bonded oxygen and hydroxyl group)
25
Q

What are the 6 functions of proteins?

A
  1. catalyze chemical reactions
  2. structural support
  3. Transportation
  4. Movement (muscle tissue)
  5. Regulation (hormones)
  6. Disease Defence (anitbodies made by immune system)
26
Q

What is the general structure of a protein?

A
  • long chains of amino acids

- unique sequence of amino aacids

27
Q

What are the 4 levels of protein organization?

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quaternary
28
Q

What is denaturation?

A

conformational change to a protein that can cause permenant or temporary changes and may cause the protein to lose its functional ability under certain circumstances

29
Q

What are the conditions for denaturation?

A

Temperature, pH and ionic concentrations

30
Q

What is a nucleic acid?

A

organic compound that carries hereditary information in cells and is composed of nucleotide monomers

31
Q

What are the main structural features of a nucleic acid?

A
  • has phosphodiester bonds
  • has backbone made of alternating sugar-phosphate-sugar-phosphate chains
  • middle is made of nitrogenous bases held by hydrogen bonds
32
Q

What are the 4 types of biochemical reactions?

A

neutralization, redox, condensation/dehydration synthesis, hydrolysis

33
Q

What Dehydration Synthesis?

A

joins monomers together to create polymers, H+OH= water. WATER IS A PRODUCT

34
Q

What is Hydrolysis?

A

breaks down polymers into monomers with addition of water. Hydrogen goes to one monomer and hydroxyl group goes to the other WATER IS A REACTANT

35
Q

What is an enzyme?

A

biological catalyst that speeds up reactions by decreasing activation energy. Usually end in “ase”

36
Q

What is activation energy?

A

the energy required to break bonds

37
Q

What is a substrate?

A

the molecule which is catalyzed by an enzyme. It attaches to the enzyme at the active site

38
Q

What is the active site?

A

where substrate binds and shape is a perfect match

39
Q

What is the enzyme-substrate complex?

A

when the substrate and the enzyme come together

40
Q

What is the induced fit model?

A

as a substrate approaches an active site, interactions between functional groups causes the protein to alter its shape to fit the substrate

41
Q

What is a coenzyme?

A

organic, assists enzymes, ex. vitamins

42
Q

What is a cofactor?

A

mineral or metal ions ex. iron, zinc, sodium

43
Q

What are the factors that affect enzyme activity?

A

Temperature and pH level

44
Q

How does temperature affect enzyme activity?

A

there is an optimum range that is relative to the organisms environment where certain enzymes can work and when they cannot

45
Q

How does pH affect enzyme activity?

A

there is an optimum range where enzymes work best at specific pH levels. Ex. pepsin in the stomach only wors at a pH of 2

46
Q

What 2 ways can you regulate enzyme activity?

A

Activators- increase activity

Inhibitors- decrease activity

47
Q

Why do you regulate enzyme activity?

A

to control biochemical pathways

48
Q

What are the 2 types of inhibition?

A

Competitive and Non-Competitive

49
Q

What is competitive inhibition?

A

inhibitor bonds at active site therefore restricting access for normal substrate

50
Q

What is non-competitive inhibition?

A

inhibitor binds to allosteric site and causes the shape of the active site ti change therefore the substrate cannot bind to the active site.

51
Q

What is the allosteric site?

A

a different location than the active site on an enzyme where other molecules or non-competitive inhibitors can bind

52
Q

What is feedback inhibition?

A

where the end product of a biochemical pathway increases and causes end product t “feedback” to allosterically inhibit a substrate at the beginning of the pathway

Grade 12 Biology (4 decks)

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