Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Year 12 Chemistry > Unit 4 AOS 2 > Flashcards

Unit 4 AOS 2 Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

What is food needed for in the body

A

energy, growth, regulating body processes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the major food groups needed for the body

A

proteins, carbohydrates, fats and oils, vitamins and minerals

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are proteins needed for

A

growth, repair, immunity, transport of molecules,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Examples of what proteins are used for

A

hormones, enzymes, cellular structures (e.g. cell membrane, muscles), to transport molecules in the body, antibodies

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What are carbohydrates needed for

A

to store and provide energy, functioning in nervous system

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are fats and oils needed for

A

insulation, to store some vitamins, to provide energy, in cell membranes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Define proteins

A

large molecules composed of one or more long chains of amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are the monomers of proteins

A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

How many amino acids are there in the body

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Can all these 20 amino acids be made by the body

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How do we get amino acids that can’t be made in our body

A

through our food

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are essential amino acids

A

amino acids that cannot be synthesised by animals from materials in their diets and therefore must be supplied directly in the diet.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What elements make up amino acids

A

C, H, O, N and sometimes S and P

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the amino acids used to synthesise proteins in the body called

A

2-amino acids or alpha amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the structure of amino acids

A

CH, R, COOH, NH2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What properties can the R chain have

A

polar, non-polar, acidic or basic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Are amino acids soluble and why

A

they are soluble as they can form H bonds with water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Can amino act as acids, bases or both

A

both

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What can amino acids act as

A

dipolar ions/zwitterions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What is a zwitterion

A

contain equal positive and negative charges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What does an amino acid look like as a zwitterion

A

NH3+ and COO-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

When does an amino acid act as a zwitterion

A

pure solid state and in aqueous solutions in neutral pH, e.g. water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What will happen to amino acid in acidic environment

A

will act as base and so will have NH3+ with COOH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What will happen to amino acid in basic environment

A

will act as an acid and so will have NH2 and COO-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What is a sequence of amino acids called

A

a peptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Between what molecules is the bond in a peptide chain

A

between the CO and the NH2 (O=C-N-H)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What is the bond in a peptide chain called

A

peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What is the name of the link between the C and the N

A

amide linkage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

When is a polypeptide called a protein

A

more than 50 amino acids/ molar mass >5000gmol-1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

How do you name a polypeptide (3)

A

by the sequence of amino acids from which they are made - which amino acid it derived from and put the abbreviation and then just put a dash to the next one, and it is written from left to right

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Where is the N-terminus in a polypeptide chain

A

left side

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Where is the C-terminus in a polypeptide chain

A

right side

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What is the amino acids components of a polypeptide called

A

amino-acid residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

Define polypeptide

A

many amino acid residues bonded together.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Define primary structure

A

the order of amino acids in a polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Define secondary structure

A

structure formed folding of the polypeptide chain due to hydrogen bonding between carboxyl and amino groups in a protein molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Important to note about secondary structure

A

the hydrogen bonding is at different positions of the chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What causes alpha helices

A

H bonding between partially partially positive NH group and the partially negative COOH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

What causes beta pleated sheet

A

H bonding between peptide links

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Define tertiary structure

A

3D structure formed from side-group interaction, including hydrogen bonding, ionic bonding, dipole–dipole interactions and disulfide bridges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Define quaternary structure

A

multiple polypeptide chains joined together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

Define denaturation

A

loss of structure or function of a protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

What causes denaturation

A

pH changes and heat

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

Why do pH changes and heat cause denaturation

A

damages bonds in polypeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Can denaturation be partial + why

A

yes if it doesn’t break primary covalent (peptide) bonds but just secondary and tertiary bonds e.g. warm milk

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Define enzymes

A

biological catalysts that speed up reactions through providing an alternate pathway for the reaction which requires less energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

What is the general suffix of enzymes

A

ase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Examples of enzymes that don’t end in ase

A

trypsin, pepsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

What are the two types of proteins

A

globular and fibrous

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

What is the solubility of globular/fibrous

A

globular is soluble and fibrous is insoluble

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

What is the lock and key model

A

the specific shape of the active site fits exactly the shape of the substrate it will act on, hence will only act on that substrate.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

What is the induced fit model

A

the specific shape of the active site of the enzyme varies slightly from that of the substrate and the two fit only after contact when the substrate induces a complementary shape at the active site of the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Define active site

A

A region on an enzyme that binds to a protein or other substance during a reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Define substrate

A

The substance on which an enzyme acts.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

Do enzymes take part in a reaction

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

Define coenzyme

A

organic non-protein molecules required to temporarily and loosely bind with the protein molecule to form an active enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

Are coenzymes specific

A

not always

58
Q

Define hydrolysis

A

the chemical breakdown of a compound due to the addition of water.

59
Q

What is the general formula for carbohydrates

A

Cx(H2O)y

60
Q

What elements do carbohydrates contain

A

C, H, O

61
Q

What is the monomer for sugars

A

monosaccharides

62
Q

Are carbohydrates soluble and why

A

due to the multiple -OH groups, they are highly soluble in water because can form H bonding

63
Q

Do all monosaccharides have the same formula

A

yes (and so are isomers)

64
Q

Can monosaccharides be linear

A

yes, but most are cyclic

65
Q

What bonds are between sugar molecules

A

ether/glycosidic links

66
Q

Where does the bond occur between monosaccharides

A

between the OH groups (and H2O is lost)

67
Q

What polymers are in starch

A

amylose and amylopectin

68
Q

Is amylose branched or linear

A

linear

69
Q

Is amylopectin branched or linear

A

branched

70
Q

What type of isomers are glucose and galactose

A

stereoisomers

71
Q

What does amylase break starch into

A

maltose

72
Q

What does maltase break maltose into

A

glucose

73
Q

What is another name for cellulose

A

fibre

74
Q

What does GI stand for

A

glycaemic index

75
Q

What is GI

A

A figure representing the relative ability of a carbohydrate food to increase the level of glucose in the blood

76
Q

Examples of food high GI

A

lollies, chocolate, ice-cream

77
Q

Examples of food low GI

A

brown rice, wholemeal bread, pasta

78
Q

How is glycaemic load calculated

A

grams in serve * GI /100

79
Q

What is the standard for GI

A

glucose at 100

80
Q

Why are fruits low GI

A

because fructose has to be converted to glucose (takes time)

81
Q

What is aspartame

A

artificial sweetener

82
Q

What are glucose blood levels measured in

A

mmol-1 (mM)

83
Q

What is called when there is too much blood glucose

A

hyperglycaemia

84
Q

What is it called when there is too little blood glucose

A

hypoglycaemia

85
Q

What are the three categories of carbohydrates

A

monosaccharides, disaccharides, polysaccharides

86
Q

What are the two types of glucose

A

alpha and beta

87
Q

Where is the OH located on alpha glucose

A

bottom

88
Q

Where is the OH located on beta glucose

A

top

89
Q

How many monomers to make polysaccharide

A

more than 10

90
Q

What are ogliosaccharides

A

Three to ten monosaccharides bonded together.

91
Q

What is the general suffix for sugars

A

ose

92
Q

How many times sweeter is aspartame compared to glucose

A

200 times sweeter

93
Q

Are amylose/amylopectin soluble/insoluble

A

amylose is soluble and amylopectin is insoluble

94
Q

General formula for glycogen

A

(C6H12O5)n

95
Q

Properties of glycogen

A

soluble, highly branched, alpha glucose

96
Q

Properties of starch

A

slightly soluble, moderately branched, alpha glucose

97
Q

Properties of cellulose

A

insoluble, unbranched, beta glucose

98
Q

Types of disaccharides (3)

A

lactose (galactose + glucose), maltose (glucose + glucose), sucrose (glucose + fructose)

99
Q

Types of polysaccharides (3)

A

starch, cellulose, glycogen

100
Q

What are vitamins

A

organic compounds that are needed in minute quantities on a regular basis as part of a healthy diet.

101
Q

How many vitamins are required by body

A

13

102
Q

Can we make vitamins

A

no, except for Vitamin D

103
Q

Two categories of vitamins

A

fat soluble and water soluble

104
Q

Examples of fat soluble vitamins

A

D, A, K, E

105
Q

Examples of water soluble vitamins

A

B, C

106
Q

Can water soluble vitamins be stored

A

no

107
Q

Where are fat soluble vitamins stored

A

in fat (adipose tissue)

108
Q

What is the only non-essential vitamin

A

Vitamin D

109
Q

What are vitamins needed for

A

regulating metabolic processes e.g. producing energy, supporting the immune system

110
Q

Are fats solids/liquids

A

solids

111
Q

Are oils solids/liquids

A

liquids

112
Q

What enzyme digests fats

A

lipase

113
Q

What is the formula for a fatty acid with 0 double bonds

A

CnH2n+1COOH

114
Q

What is the formula for a fatty acid with 1 double bond

A

CnH2n-1COOH

115
Q

What is the formula for a fatty acid with 2 double bonds

A

CnH2n-3COOH

116
Q

What are fatty acids

A

long-chain carboxylic acid containing an even number of carbon atoms.

117
Q

Saturated fatty acid

A

no double bonds

118
Q

Mono-unsaturated fatty acid

A

1 double bond

119
Q

Polyunsaturated fatty acid

A

more than 1 double bond

120
Q

What is the link called in a fatty acid

A

ester link

121
Q

What are the essential fatty acids of the body

A

alpha-linolenic acid (ALA) and linoleic acid (LA).

122
Q

What are essential fatty acids also called

A

omega fatty acids

123
Q

What is omega 3 fatty acid

A

alpha-linolenic acid

124
Q

What is omega 6 fatty acid

A

linoleic acid

125
Q

What is the order of energy sources in body

A

carbohydrates, then fats then proteins

126
Q

Are saturated or unsaturated more likely to go rancid

A

unsaturated as less stable

127
Q

What is the omega group in fatty acid

A

methyl

128
Q

What emulsion

A

breaking down fats (bile)

129
Q

What is calorimetry

A

Method used to determine the changes in energy of a system by measuring heat exchanges with the surroundings. It is the measurement of the amount of heat released or absorbed in a chemical reaction, change of state or formation of a solution.

130
Q

What is a calorimeter

A

Apparatus used to measure heat changes during a chemical reaction or change of state.

131
Q

What are different types of calorimeters

A

bomb calorimeters and solution calorimeters

132
Q

Formula for energy in calorimetry (2)

A

E = V * I * t or E = n * delta H

133
Q

What is metabolism

A

chemical processes that involve breaking down and building different substances

134
Q

What is calibration factor

A

the amount of energy that is required to change the contents of the calorimeter by 1 degree

135
Q

Formula for calibration factor in calorimetry

A

Cf = E/delta T

136
Q

Unit for calibration factor

A

J / degrees Celsius

137
Q

Is calories with a lower case c or upper case c

A

lower case c

138
Q

Is it usually cis or trans in unsaturated fatty acids

A

cis

139
Q

What is the functional group of monosaccharides

A

OH

140
Q

What type of double bond (cis or trans) occurs in nature

A

cis

141
Q

Can trans bonds occur in nature

A

no

Year 12 Chemistry (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions