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a level biology > Chapter 1 > Flashcards

Chapter 1 Flashcards

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AP® Biology flashcards
1
Q

What is a molecule ?

A

two or more atoms bonded together to form a single chemical entity

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2
Q

What is a covalent bond ?

A

Is a force of attraction between a nuclei and the shared pair of electrons

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3
Q

What is an ionic bond ?

A

Is a force of electrostatic attraction between oppositely charged ions

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4
Q

What is a hydrogen bonding ?

A

A special type of attraction between molecules to a hydrogen atom

Has to be O , N , F

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5
Q

What is the polymer of amino acids ?

A

Polypeptides

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6
Q

What is the polymer of monosaccharides ?

A

Polysaccharides

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7
Q

What is a polymer of nucleotides ?

A

Polynucleotides

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8
Q

What is a condensation reaction ?

A

The release of water when a monomer is added chemically to a polymer

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9
Q

What is a hydrolytic reaction ?

A

Add water to cause a release of a monomer from a polymer

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10
Q

Metabolism definition

A

All of the chemical processes that take place in living organisms

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11
Q

Characteristics of monosaccharides

A

Sweet tasting, soluble in water (CH2O)n

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12
Q

Colour results of Benedict’s test

A

Red = high
Brown = medium
Yellow = low
Green = very low
Blue = none

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13
Q

Maltose

A

Alpha glucose + alpha glucose

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14
Q

Lactose

A

Alpha glucose + galactose

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15
Q

Sucrose

A

Alpha glucose + fructose

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16
Q

What bond do monosaccharides form

A

Glycosidic

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17
Q

Learn alpha and beta glucose structure and maltose

A
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18
Q

Test for sucrose

A

Hydrolyse the disaccharide using HCl and a boiling water bath
Slowly add NaHCO3 to neutralise the HCl until the solution is alkaline (test with blue litmus paper)
Carry out Benedict’s test

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19
Q

Test for starch

A

Iodine solution
High = blue/black
Low = red/brown

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20
Q

Starch structure and function
(5 things)

A

Insoluble so doesn’t affect water potential and osmosis
Large and insoluble
Coiled into a helix
Hydrolysed to alpha glucose
Branched version has many ends for attack and rapid release of alpha glucose

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21
Q

Glycogen structure and function
(3 things)

A

Insoluble so doesn’t affect water potential of the cell
Coiled into a helix making it compact
Highly branched

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22
Q

Cellulose structure

A

Beta glucose chains form microfibrils which form cellulose fibres

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23
Q

5 roles of lipids

A

Cell membranes, energy, waterproofing, insulation and protection

24
Q

What is the general structure of lipids

A

Three fatty acids attached to one glycerol

25
Q

What bond links the fatty acids and glycerol

A

Ester bond

26
Q

What determines the saturation

A

Presence and number of carbon to carbon double bonds
Unsaturated = one or more

27
Q

Structure and properties of triglycerides

A

Energy dense, insoluble so no effect on water potential, large, non-polar

28
Q

What is a phospholipid

A

A triglyceride with one fatty acid replaced by phosphate group

29
Q

Hydrophilic definition

A

Water loving

30
Q

Hydrophobic definition

A

Water hating

31
Q

What do phospholipids do ?

A

Forms a phospholipid bilayer in cell membranes, creates a hydrophobic barrier between inside and outside of cell

32
Q

Emulsion test

A

2cm of ethanol and 2cm of sample poured into 5 cm of distilled water. Positive = loudy
Negative = clear

33
Q

What bond joins amino acids

A

Peptide bonds

34
Q

What’s the primary structure of proteins

A

The sequence of amino acids in the polypeptide chains

35
Q

Secondary structure of proteins

A

When the chain is coiled into alpha helices

36
Q

What is the tertiary structure of proteins

A

The folding and twisting of the polypeptide chain

37
Q

Quarternary structure of proteins

A

More than 1 polypeptide chain and/or a prosthetic group

38
Q

How does the tertiary structure of protein happen?

A

Bonds are between the R-groups of amino acids.
3 bonds: disulphide bridges, ionic bonds, hydrogen bonds

39
Q

Test for protein

A

Biuret test detects peptide bonds
Positive = purple
Negative = blue

40
Q

Enzyme definition

A

biological catalysts, that speed up and control chemical reactions in the body, without being changed by the reaction

41
Q

Substrate definition

A

Material which is catalysed by the enzyme

42
Q

Active site definition

A

Area of the enzyme where the substrate will bind during the reaction

43
Q

Enzyme substrate complex

A

Temporary bound combination of enzyme and substrate before reaction occurs

44
Q

Enzyme product complex

A

Temporary bound combination of enzyme and product after reaction occurs

45
Q

What’s the lock and key theory of enzyme action

A

Enzymes are specific to one substrate and the teeth of the key are the active site

46
Q

What’s the modern enzyme theory model

A

Induced-fit model

47
Q

What’s the induced-fit model

A

The active site forms it’s shape as it interacts with the substrate. As the enzyme changes shape it puts a strain on the substrate causing a strain on particular bonds

48
Q

What two conditions are necessary for enzymes to work ?

A

Physical contact with the substrate, active site with specific shape to fit substrate

49
Q

Effect of temp on enzyme rate
(3 points)

A

As temp increases, the rate of enzyme activity increases as the temp increases the kinetic energy of the particles and increases the number of successful collisions between substrate and enzyme until the optimum temp then the enzymes become denatured

50
Q

Effect of pH on enzyme action
(2 points)

A

As pH increases the rate of enzyme activity increases until the optimum pH where it is at its most effective.
As pH increases above the optimum pH true rate of enzyme activity decreases

51
Q

Effect of enzyme concentration on the rate of reaction

A

As the enzyme concentration increases, the initial rate of reaction increases

52
Q

Effect of substrate concentration on the rate of enzyme action

A

As substrate concentration increases, the reaction rate increases more substrate equals more collisions with the enzyme. Our substrate concentration continues to increase. The reaction remains constant because all enzyme active sites are occupied by substrate

53
Q

Where does competitive inhibition bind?

A

Binds to active site

54
Q

Consequence of competitive inhibition

A

Active site is occupied so substrate cannot bind

55
Q

Where do noncompetitive inhibitors bind ?

A

Binds to a different part of the enzyme

56
Q

What is the consequence of noncompetitive inhibition?

A

The active site has a different shape so substrate cannot bind

a level biology (20 decks)

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