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AS Biology > Biological Molecules > Flashcards

Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

types of functional groups in carbohydrates (2)

A

aldehyde, ketone

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2
Q

formula & shape of aldehyde group

A

CHO

O
||
C – H

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3
Q

formula &shape of ketone group

A

CO

C=O

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4
Q

name of sugars containing ketone group

A

ketoses

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5
Q

name of sugars containing aldehyde group

A

aldoses

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6
Q

GLUCOSE

name of ring form

A

hexagonal 5-carbon pyranose ring

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7
Q

GLUCOSE

aldose or ketose sugar?

A

aldose

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8
Q

GLUCOSE

function

A

used to make ATP during respiration, animals

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9
Q

GLUCOSE

mode of transport, animals

A

blood (dissolved in plasma)

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10
Q

GLUCOSE

why is it easy to transport?

A

water-soluble

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11
Q

FRUCTOSE

formula

A

C6H12O6

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12
Q

FRUCTOSE

source

A

fruits

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13
Q

FRUCTOSE

name of ring form

A

pentagonal 4-carbon furanose

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14
Q

GLUCOSE

alpha glucose - diagram

A

OH is below the plane of the ring (on the right side):

H
 |
C
 |
OH
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15
Q

GLUCOSE

beta glucose - diagram

A

OH is above the plane of the ring (on the right side)

OH
  |
 C
  |
 H
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16
Q

FRUCTOSE

aldose or ketose?

A

ketose

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17
Q

FRUCTOSE

why does it have same formula as glucose?

A

is an isomer

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18
Q

GALACTOSE

formula

A

C6 H10 O6

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19
Q

GALACTOSE

source

A

milk

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20
Q

GALACTOSE

ring form

A

pyranose

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21
Q

GALACTOSE

aldose or ketose?

A

aldose

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22
Q

GALACTOSE

difference from glucose

A

OH on left side above the plane of the ring

OH
  |
 C
  |
 H

instead of

H
 |
C
 |
OH
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23
Q

MALTOSE

reactant molecules

A

2 alpha glucoses

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24
Q

MALTOSE

type of reaction that forms it

A

condensation

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25
Q

MALTOSE

name of connecting bond

A

1,4 alpha-glycoside

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26
Q

SUCROSE

reactant molecules

A

alpha glucose & fructose

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27
Q

SUCROSE

type of reaction

A

condensation

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28
Q

SUCROSE

function

A

respiration in plants

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29
Q

SUCROSE

transport, plants

A

phloem sap (dissolved)

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30
Q

STARCH

function

A

energy storage, plants

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31
Q

STARCH

general formula

A

(C6 H12 O5)n

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32
Q

STARCH

polysaccharides

A

amylose, amylopectin

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33
Q

STARCH

ratio of amylose to amylopectin

A

1:4

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34
Q

AMYLOSE

% of starch

A

20%

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35
Q

AMYLOSE

monomer unit

A

alpha glucose

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36
Q

AMYLOSE

2 features

A

unbranched chains

helical structure

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37
Q

AMYLOSE

linkage

A

1,4 alpha-glycosidic

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38
Q

AMYLOSE

reason for stability

A

H bonds

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39
Q

AMYLOPECTIN

% of starch

A

80

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40
Q

AMYLOPECTIN

monomer

A

alpha glucose

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41
Q

AMYLOPECTIN

structure

A

branched

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42
Q

AMYLOPECTIN

linkage

A

1,4 & 1,6 alpha glycosidic

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43
Q

AMYLOPECTIN

strength of hydrogen bonds

A

weak

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44
Q

AMYLOPECTIN

reason for reactivity

A

branched & unstable structure = easy to break bonds

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45
Q

AMYLOPECTIN

benefit of being in larger proportion than amylose

A

starch is easy to digest & break down

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46
Q

GLYCOGEN

general formula

A

(C6 H12 O5)n

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47
Q

GLYCOGEN

function

A

storage of sugar in animals

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48
Q

GLYCOGEN

how is it created?

A

glucose –> glycogen in presence of insulin

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49
Q

GLYCOGEN

structural features

A

highly branched

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50
Q

GLYCOGEN

monomer unit

A

alpha glucose

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51
Q

GLYCOGEN

linkages

A

1,4 & 1,6 alpha-glycosidic

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52
Q

GLYCOGEN

3 benefits of using as a storage molecule in humans

A

highly branched = v. compact & easy to break down

insoluble in water

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53
Q

GLYCOGEN

benefit of being insoluble

A

osmotic potential of tissue fluid maintained; difficult to move around by accident (makes storage easy)

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54
Q

CELLULOSE

location

A

plant cell walls

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55
Q

CELLULOSE

monomer

A

beta glucose

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56
Q 
CELLULOSE
structure (4)
A

unbranched. straight chains, parallel to each other
180 degree face reversal of alternate glucose molecules
v. strong hydrogen bonds

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57
Q

CELLULOSE

linkage

A

1,4 beta glycosidic

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58
Q

CELLULOSE

no. of glucose units in single chain

A

60-70

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59
Q

CELLULOSE

formation of cell wall (sequence)

A

chains -> microfibrils -> macrofibrils -> cell wall

60
Q

monomers of lipids

A

glycerol; fatty acids

61
Q

FATTY ACIDS

saturated

A

all C molecules are bonded to an atom; no free carbon molecules left

62
Q

FATTY ACIDS

unsaturated

A

contain C=C

63
Q

FATTY ACID

state at rtp (saturated)

A

solid

64
Q

FATTY ACID

state at rtp (unsaturated)

A

liquid

65
Q

TRIGLYCERIDES

reactant molecules

A

1 glycerol; 3 fatty acids

66
Q

TRIGLYCERIDES

type of reaction

A

condensation

67
Q

TRIGLYCERIDES

molecules of water formed

A

3

68
Q

TRIGLYCERIDES

name of linkage

A

ester

69
Q

TRIGLYCERIDES

advantage as an energy source

A

3x more energy derived than carbohydrates

70
Q

TRIGLYCERIDES

disadvantage as an energy source

A

more difficult to break down

71
Q

TRIGLYCERIDES

calorific value

A

36.4 kJ

72
Q

TRIGLYCERIDES

use in plants (1)

A

formation of waxy cuticle to make leaves waterproof

73
Q

TRIGLYCERIDES

use in animals (2)

A

production of metabolic water; thermal insulation

74
Q

PHOSPOLIPIDS

structure

A

1 glycerol; 2 fatty acids; 1 phospate group

75
Q

PHOSPOLIPIDS

properties

A

hydrophyllic ends facing in

76
Q

PHOSPHOLIPIDS

composition

A

1 glycerol; 2 fatty acids; 1 phospate group

77
Q

PHOSPHOLIPIDS

properties

A

hydrophilic heads

hydrophobic tails

78
Q

PHOSPHOLIPIDS

arrangement in the cell membrane

A

bilayer; heads facing outwards

O==O
O==O
O==O

79
Q

PHOSPHOLIPIDS

types of fatty acids present in tail

A

unsaturated & saturated

80
Q

PHOSPHOLIPIDS

impact of unsaturated fatty acids being present in bilayer

A

prevent the phospholipids from bunching too close together; the cell membrane remains fluid

81
Q

CHOLESTROL

role in cell membrane (3)

A
  1. regulates membrane fluidity by disrupting the regular pattern of phospholipids;
  2. prevents close packing of phospholipids at low temperatures
  3. limits uncontrolled leakage of small ions & water from the cell
82
Q

CHOLESTROL

role in cell membrane (3)

A
  1. regulates membrane fluidity by disrupting the regular pattern of phospholipids;
  2. prevents close packing of phospholipids at low temperatures
  3. limits uncontrolled leakage of small ions & water from the cell
83
Q

PROTEINS

definition

A

organic compounds made of amino acids

84
Q

AMINO ACIDS

definition

A

monomers of proteins

85
Q 
AMINO ACIDS
groups present (2)
A

amine; carboxylic

86
Q

AMINO ACIDS

formula of amine group

A

NH2

87
Q

AMINO ACIDS

formula of carboxylic group

A

COOH

88
Q

AMINO ACIDS

ways to classify (4)

A

essential/non-essential
R group - present or absent
acidity vs. basicity
polarity

89
Q

AMINO ACIDS

essential - meaning

A

not made in the body; have to be derived from other sources

90
Q

AMINO ACIDS

non-essential - meaning

A

made in the body

91
Q

AMINO ACIDS

which one doesn’t have an R group?

A

glycine

92
Q

AMINO ACIDS

what does glycine have instead of an R group?

A

H

93
Q

AMINO ACIDS

shortest amino acid

A

glycine

94
Q

AMINO ACIDS

cause for negative polarity

A

COOH group loses a hydrogen atom

95
Q

AMINO ACIDS

cause for positive polarity

A

amine group gains a hydrogen atom

96
Q

AMINO ACIDS

zwitter ion

A

charged amino acid whose overall polarity is zero

97
Q

AMINO ACIDS

zwitter ion - formation

A

both amine & carboxylic groups gain & lose H atoms

98
Q

AMINO ACIDS

acidic

A

R group contains COOH

99
Q

AMINO ACIDS

basic

A

R group contains NH4

100
Q

AMINO ACIDS

reaction through which they combine

A

condensation

101
Q

AMINO ACIDS

name of linkage

A

peptide bond

102
Q

AMINO ACIDS

name of peptide bond between two amino acids

A

dipeptide

103
Q

AMINO ACIDS

name of peptide bond between three amino acids

A

tripeptide

104
Q

POLYPEPTIDE

definition

A

a protein molecule made up of many amino acids linked to each other through a peptide bond

105
Q

POLYPEPTIDE

reaction that breaks them down

A

hydrolysis

106
Q

PROTEINS

where are they synthesised?

A

ribosome

107
Q

PROTEINS

where are they synthesised?

A

ribosome

108
Q

PROTEINS: PRIMARY STRUCTURE

primary structure - definition

A

linear sequence of amino acids in a polypeptide chain

109
Q

PROTEINS: PRIMARY STRUCTURE

primary structure - linkage

A

peptide bonds

110
Q

PROTEINS: PRIMARY STRUCTURE

how can it be broken?

A

hydrolysis/enzymes

111
Q

PROTEINS: SECONDARY STRUCTURE

definition

A

structure that refers to the 3D arrangement of the main chain atoms

112
Q

PROTEINS: SECONDARY STRUCTURE

how is it kept stable?

A

hydrogen bonds between molecules

113
Q

PROTEINS: SECONDARY STRUCTURE

types (2)

A

alpha helix; beta-pleated sheet

114
Q

PROTEINS: TERTIARY STRUCTURE

definition

A

structure that refers to the 3D arrangement of ALL the atoms in a protein

115
Q

PROTEINS: TERTIARY STRUCTURE

types of bonds (4)

A

hydrogen; ionic; hydrophobic; disulfide

116
Q

PROTEINS: TERTIARY STRUCTURE

types of bonds (4)

A

hydrogen; ionic; hydrophobic; disulfide bridges

117
Q

PROTEINS: TERTIARY STRUCTURE

examples of strongly polar groups

A

–NH–, –CO–, –OH

118
Q

PROTEINS: TERTIARY STRUCTURE

when can hydrogen bonds break?

A

at high temperatures & pH

119
Q

PROTEINS: TERTIARY STRUCTURE

where do hydrophobic interactions occur?

A

between non-polar R groups

120
Q

PROTEINS: TERTIARY STRUCTURE

why do hydrophobic groups stay together?

A

are repelled by water env. around them

121
Q

PROTEINS: TERTIARY STRUCTURE

where do ionic bonds form?

A

between ionized amine and carboxylic groups

122
Q

PROTEINS: TERTIARY STRUCTURE

how can ionic bonds be broken?

A

by changes in pH

123
Q

PROTEINS: TERTIARY STRUCTURE

diff. b/w ionic & hydrogen bonds

A

hydrogen: form between partially charged groups
ionic: form between fully ionised groups

124
Q

PROTEINS: TERTIARY STRUCTURE

between which amino acids does a disulfide bridge form?

A

cysteine

125
Q

PROTEINS: TERTIARY STRUCTURE

element involved in disulfide bridges

A

sulphur

126
Q

PROTEINS: TERTIARY STRUCTURE

how can disulfide bridges be broken?

A

by a reducing agent (2H removed)

127
Q

PROTEINS: TERTIARY STRUCTURE

arrangement of bonds acc. to strength (weak to strong)

A

hydrophyllic < hydrogen < ionic < disulfide

128
Q

PROTEINS: TERTIARY STRUCTURE

arrangement of bonds acc. to strength (weak to strong)

A

hydrophobic < hydrogen < ionic < disulfide

129
Q

PROTEINS: TERTIARY STRUCTURE

molecules in a fibrous protein: shape

A

long and thin

130
Q

PROTEINS: TERTIARY STRUCTURE

molecules in a fibrous protein: arrangement

A

rows, parallel to each other (form fibrils)

131
Q

PROTEINS: TERTIARY STRUCTURE

molecules in a fibrous protein: solubility

A

not soluble in water

132
Q

PROTEINS: TERTIARY STRUCTURE

fibrous proteins - role: structural or metabolic?

A

stuctural

133
Q

PROTEINS: TERTIARY STRUCTURE

fibrous proteins: 2 examples + location

A

collagen: outer walls of arteries & veins
keratin: hair and fingernails

134
Q

PROTEINS: COLLAGEN

no. of polypeptide chains

A

3 (triple helical)

135
Q 
PROTEINS: COLLAGEN
primary structure (2)
A

repetitive sequence of amino acids; every 3rd amino acid is glycine

136
Q

PROTEINS: COLLAGEN

which bond stabilises the structure?

A

H–H

137
Q

PROTEINS: COLLAGEN

main function

A

to provide support & elasticity in animal tissues

138
Q

PROTEINS: COLLAGEN

reason for insolubility

A

molecules too large and long to dissolve in water

139
Q

PROTEINS: COLLAGEN

benefit of having 3 polypeptide chains

A

high tensile strength

140
Q

PROTEINS: COLLAGEN

meaning of high tensile strength

A

can stretch slightly & withstand large pulling forces without breaking

141
Q

PROTEINS: COLLAGEN

benefit of having glycine as a repeating unit

A

compactness = chains pack together strongly

142
Q

PROTEINS: COLLAGEN

role of lysine

A

formation of cross-links between molecules = formation of fibrils & fibres of collagen

143
Q

PROTEINS: GLOBULAR PROTEINS

shape

A

spherical

144
Q

PROTEINS: GLOBULAR PROTEINS

arrangement of molecules

A

hydrophobic amino acids face inwards; hydrophobic amino acids face outwards

145
Q

PROTEINS: GLOBULAR PROTEINS

solubility

A

soluble

146
Q

PROTEINS: GLOBULAR PROTEINS
function: structural or metabolic?

A

metabolic

147
Q

PROTEINS: GLOBULAR PROTEINS

examples + location

A

Hb - blood

salivary amylose - salivary gland/mouth

AS Biology (5 decks)

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