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biology module 2- foundations in biology > 2.2 biological molecules > Flashcards

2.2 biological molecules Flashcards

1
Q

nutrients are broken down by

A

digestion

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2
Q

anabolic reactions are where

A

products of digestion are digested into the blood stream and used to make larger molecules

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3
Q

metabolism is

A

the sum of all chemical reactions taking place in an organism

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4
Q

why is carbon so abundant in biomols

A

it can form 4 strong covalent bonds, it is very versatile

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5
Q

in condensation reactions, - join together to form a -

A

monomers join together to form a polymer

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6
Q

a water molecule is released in

A

condensation reactions

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7
Q

a covalent bond is made in

A

condensation reactions

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8
Q

a water molecule is used in

A

hydrolysis reactions

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9
Q

a covalent bond is broken in

A

hydrolysis reactions

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10
Q

hydrolysis reactions split - into -

A

polymers into monomers

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11
Q

carbohydrates monomer is

A

monosaccharides

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12
Q

carbohydrates polymer is

A

polysaccharides

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13
Q

proteins monomer is

A

amino acids

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14
Q

proteins polymer is

A

polypeptides

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15
Q

nucleic acids monomer is

A

nucleotides

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16
Q

nucleic acids polymer is

A

DNA and RNA

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17
Q

water is a - molecule

A

polar

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18
Q

bonds in water are

A

hydrogen bonds

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19
Q

the density of water is

A

997kg/m3

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20
Q

water is most dense at

A

4 degrees c

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21
Q

the density of water makes it a good…

A

habitat, as ice floats on its surface

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22
Q

what are adhesive properties

A

molecules are highly attracted to other molecules

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23
Q

does water have adhesive properties

A

yes

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24
Q

water’s adhesive properties make it a good… because…

A

transport medium, they create a pull on the water column, which plants use to transport water from roots to leaves

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25
Q

water has a surface tension of - at room temperature

A

72mN/m

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26
Q

the high surface tension of water makes it a good - because…

A

habitat, insects can float on the surface and carry out actions there

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27
Q

water has a - latent heat of vaporisation

A

high

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28
Q

the high latent heat of vaporisation of water makes it a good- because…

A

means of temperature regulation because it means it can be used in humans for their sweat without it vaporising too easily, causing excessive sweating

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29
Q

water has a specific heat capacity of…

A

4200J/kg c

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30
Q

water has a - specific heat capacity

A

high

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31
Q

water’s high specific heat capacity means it is useful in

  1. because…
  2. because …
A
  1. means of temperature regulation, heat can be stored in water and then used to regulate the temperature of nearby land at the coastline
  2. transport medium, it can retain heat and then distribute it through warm blooded animals
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32
Q

water molecules have a - arrangement of - and - atoms

A

polar, hydrogen and oxygen

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33
Q

hydrogen is - charged, so attracts things which are -

A

positively, negative

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34
Q

oxygen is - charged, so attracts things which are -

A

negatively, positive

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35
Q

water being a polar molecule makes it a good - because…

A

solvent, it can strongly attract other molecules, disrupting the forces of attraction between molecules and dissolving them

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36
Q

water has a - latent heat of fusion

A

high

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37
Q

does water freeze easily?

A

no

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38
Q

water’s high latent heat of fusion makes it a good - because…

A

habitat, it doesn’t freeze too easily

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39
Q

water’s appearance is…

A

clear and colourless

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40
Q

water’s appearance makes it a good - because…

A

habitat, light can reach organisms living in the water

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41
Q

water is very - so can…

A

viscous, slide easily

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42
Q

waters viscosity makes it a good - because

A

means of transport because structures can easily move through it to transport materials

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43
Q

carbohydrates role in the body

A

energy in respiration

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44
Q

proteins role in the body

A

growth and repair, enzymes, antibodies, hormones

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45
Q

lipids role in the body

A

insulation, fatty cell membranes, electrical insulation

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46
Q

vitamins and minerals role in the body

A

coenzymes and activators, form parts of larger molecules

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47
Q

nucleic acids role in the body

A

carry the genetic code

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48
Q

water role in the body

A

keep cells turgid, provide a site for chemical reactions

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49
Q

what is a covalent bond

A

a strong bond made between 2 atoms formed by the sharing of electrons

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50
Q

what type of bonding is present within a water molecule?

A

covalent

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51
Q

what type of bonding is present between water molecules?

A

hydrogen

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52
Q

what 3 types of substance dissolve easily in water

A
  1. soluble substances
  2. polar molecules
  3. hydrophilic materials
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53
Q

monosaccharides general formula

A

Cn (H2O)n

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54
Q

how many carbon atoms in a triose sugar

A

3

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55
Q

how many carbon atoms in a pentose sugar

A

5

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56
Q

how many carbon atoms in a hexose sugar

A

6

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57
Q

the monosaccharides found in DNA and RNA are - sugars

A

pentose

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58
Q

all monosaccharides are - sugars

A

reducing

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59
Q

monosaccharides can reduce - in - to-

A

blue cu2+ ions in Benedict’s reagent to red cu+ ions

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60
Q

properties of monosaccharides are…

A

sweet, water soluble, form crystals

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61
Q

glucose molecules contain many bonds which can be - during - to -

A

broken down, respiration, release energy

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62
Q

energy released from glucose is used to

A

make ATP

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63
Q

break down of glucose in living organisms occurs in a series of

A

enzyme controlled steps

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64
Q

if the hydroxyl group is below, it is

A

alpha glucose

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65
Q

is the hydroxyl group is above, it is

A

beta glucose

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66
Q

which type of glucose can be used in respiration

A

alpha glucose

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67
Q

why can’t animals use beta glucose?

A

because they have enzymes which can only break down the shape of alpha glucose

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68
Q

what do you use to test for reducing sugars

A

Benedict’s reagent

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69
Q

if glucose is present, Benedict’s reagent goes from

A

blue to red or blue- green- yellow- orange- red

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70
Q

monosaccharides join together in - reactions to form - then -

A

condensation, disaccharides, polysaccharides

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71
Q

when monosaccharides join together in condensation reactions, they form a - and - is produced

A

glycosidic bond, water

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72
Q

maltose and lactose are

A

reducing sugars

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73
Q

sucrose is a

A

non reducing sugar

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74
Q

examples of disaccharides are

A

maltose, lactose, sucrose

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75
Q

can sucrose reduce the Cu2+ in Benedict’s reagent?

A

no

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76
Q

for sucrose to reduce the Cu2+ in Benedict’s reagent, it must first be…

A

hydrolysed by acid

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77
Q

maltose is - with Benedict’s reagent

A

positive

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78
Q

lactose is - with Benedict’s reagent

A

positive

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79
Q

sucrose is initially - with Benedict’s reagent

A

negative

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80
Q

sucrose is - with Benedict’s reagent once it has been hydrolysed by acid

A

positive

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81
Q

glucose + glucose —>

A

maltose

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82
Q

glucose + fructose —>

A

sucrose

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83
Q

maltose has a - bond

A

alpha 1-4 glycosidic

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84
Q

sucrose has a - bond

A

alpha 1-2 glycosidic

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85
Q

what are polysaccharides?

A

polymers containing many monosaccharides

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86
Q

polysaccharides contain - bonds

A

glycosidic

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87
Q

polysaccharides are formed by - reactions

A

condensation

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88
Q

all polysaccharides are -, so make good…

A

insoluble, storage molecules and building materials

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89
Q

starch function

A

energy storage in plants

90
Q

starch is a

A

heteropolysaccharide

91
Q

starch is a mixture of the 2 polysaccharides

A

amylose and amylopectin

92
Q

amylose contains - bonds

A

alpha 1-4 glycosidic

93
Q

amylose is a chain of

A

alpha glucose monomers

94
Q

amylose coils to form a…

A

Compact helical structure

95
Q

In amylose - bonds are holding its shape

96
Q

In amylose, the - groups on the outside can form - bonds with water, so amylose is

A

OH, H, soluble

97
Q

Amylopectin has faster reactions as…

A

it has more ends to be hydrolysed

98
Q

Amylopectin is made from

A

Glucose monomers

99
Q

Amylopectin is branched because

A

It contains both 1-4 and 1-6 glycosidic bonds

100
Q

How do you test for starch?

101
Q

When starch is present, iodine goes from - to-

A

Brown - blue/ black

102
Q

Glycogen function

A

Energy storage in animals

103
Q

Glycogen is made from

A

Alpha glucose monomers

104
Q

Glycogen is similar in structure to

A

Amylopectin

105
Q

glycogen is a

A

polysaccharide

106
Q

glycogen contains more - bonds than amylopectin

A

1-6 glycosidic

107
Q

does glycogen leave the cell? why?

A

no, it is too large

108
Q

is glycogen soluble

109
Q

glycogen does not affect

A

osmotic potential

110
Q

cellulose is found in

A

plant cell walls

111
Q

cellulose is made from

A

beta glucose monomers

112
Q

cellulose contains - bonds

113
Q

the bonds in cellulose are WEAK or STRONG

114
Q

in cellulose, glucose monomers alternate their - by

A

orientation, 180 degrees

115
Q

in cellulose, - is removed

116
Q

cellulose is - because there are no - groups present to from - bonds with

A

insoluble, OH, hydrogen

117
Q

cellulose have strong linear chains which form layered - which are crossed together by more - bonds to form -

A

microfibrils, hydrogen, macrofibres

118
Q

the strong structure of cellulose is used to…

A

give the plant strength, structural support and rigidity

119
Q

the basic monomer unit of proteins is

A

amino acids

120
Q
  • reactions link amino acids together into a - by forming a – bond and releasing -
A

condensation, dipeptide, covalent peptide, water

121
Q

the addition of another amino acid to a dipeptide creates a -

A

polypeptide

122
Q

how many R groups are there

123
Q

what is the carboxyl group in proteins

124
Q

in amino acids, the only thing that separates them is the -

125
Q

some R groups can be - or -

A

charged or hydrophilic/ hydrophobic

126
Q

define amphoteric

A

something with both acidic and basic properties

127
Q

which amino acid has sulfur in its R group?

128
Q

how do we test for proteins

A

with biuret reagent

129
Q

plants can manufacture all of their amino acids using - from -

A

nitrogen from the soil

130
Q

animals can only make some amino acids, so they need to get some from their -

131
Q

can animals store excess amino acids?

132
Q

animals can’t store excess amino acids because…

A

their amino groups make them toxic

133
Q

what is deamination

A

when the amino group is removed from amino acids

134
Q

amino acids are converted to - and excreted via the -

A

urea, kidney

135
Q

peptide bonds are between - and -

A

carbon and nitrogen

136
Q

biuret’s reagent goes from - to - if protein is present

A

pale blue to purple

137
Q

protein reduces the - ions in biurets to - ions

A

cu2+ to cu+

138
Q

covalent peptide bonds are broken down by

A

protease enzymes

139
Q

formation and breakage of peptide bonds in organisms is controlled by

140
Q

what digests protein in the stomach

141
Q

proteases regulate the breakdown of - so that their effects are not permanent

A

protein hormones

142
Q

what 2 groups make an amino acid amtopheric?

A

basic amino group and acidic carboxyl group

143
Q

the amino group has - and -

A

hydrogen and nitrogen

144
Q

insulin function

A

controls blood glucose levels

145
Q

haemoglobin fuction

A

transferring oxygen from the lungs to the tissues

146
Q

Catalase function

A

Neutralisation of hydrogen peroxide through decomposition

147
Q

name three globular proteins

A

insulin, haemoglobin, catalase

148
Q

insulin structure

A

A protein composed of two chains (an A and B chain) linked together by Sulphur atoms

149
Q

haemoglobin structure

A

Haemoglobin is composed of four polypeptides – two alpha, two beta

150
Q

catalase structure

A

It is a tetrameric enzyme, consisting of four, identical tetrahedrally arranged subunits of 60 kDa (way of expressing molecular mass).

151
Q

how does catalase’s structure help its function

A

The presence of of the iron II atoms in the prosthetic groups allow catalase to interact with hydrogen peroxide and speed up its breakdown.

152
Q

how does insulin’s structure help its function

A

allows it to be soluble, which means it can travel in the bloodstream

153
Q

how does haemoglobin’s structure help its function

A

the Fe2+ ions present in the structure can each combine reversibly with an oxygen molecule, allowing it to transport oxygen around the body.

154
Q

insulin specific groups

A 
Rapid-acting insulin.
Short-acting insulin.
Intermediate-acting Insulin.
Mixed insulin.
Long-acting insulin.
155
Q

haemoglobin specific groups

A

Haemoglobin S
Haemoglobin C
Haemoglobin E
Haemoglobin D

156
Q

catalase specific groups

A

Monofunctional
heme-containing catalases
Heme-containing catalase-peroxidases
Manganese-containing catalases

157
Q

name the 3 fibrous proteins

A

keratin, collagen, elastin

158
Q

collagen function

A

a connective tissue found in the skin, tendons, ligaments and the nervous system

159
Q

keratin function

A

providing flexibility in hair and nails, found on the lining of tissues

160
Q

elastin function

A

allows heart vessels and alveoli to stretch under high pressure and then return to their regular shape

161
Q

collagen structure

A
  • triple helix of 3 tightly wound chains

- proline, hydroxyproline and glycine

162
Q

elastin structure

A
  • cross-linked strands with hydrophobic regions
163
Q

level of protein structure of globular proteins

A

quarternary

164
Q

elastin level of protein structure

A

quarternary

165
Q

keratin structure

A

four alpha helical segments cross-linked by 3 beta chains

166
Q

collagen role of structure in function

A

the tightly wound chains of amino acid create strong, long and thin fibrils which can be used to provide elasticity to the skin and to protect softer tissues.

167
Q

elastin role of structure in function

A

the hydrophobic areasassociate, causing elastinmolecules to group together.When stretched these strandsmoveapart but remain attached at the crosslinks. After stretching, the elastin molecules reassociate, springing back together.

168
Q

keratin role of structure in function

A

cysteine in keratin is used to form disulphidebonds- these are strong covalent bonds. This helps as it makes keratin strong.

169
Q

the sequence of amino acids in a polypeptide is called the

A

primary structure

170
Q

the 2 secondary structures are…

A

alpha helix and beta pleated sheet

171
Q

the tertiary structure is…

A

the secondary structures coiled together

172
Q

the bonds responsible for holding the tertiary structure can be

A

disulfide bonds, ionic bonds, hydrogen bonds and hyrophobic and hydrophillic interactions

173
Q

a quarternary structure is where

A

a protein is made from more than one polypeptide

174
Q

state some functions of lipids

A

energy, insulation in blubber, hormones as steroids, hibernation for energy and warmth, electrical insulation in the myelin sheath, membranes as phospholipids

175
Q

lipids are all made from -, - and - atoms

A

C, H and O

176
Q

lipids are soluble in - but insoluble in -

A

organic solvents, water

177
Q

lipids are all called - because they are made from at least 2 different molecules

A

macromolecules

178
Q

lipids make up -% of the organic matter in a cell

179
Q

triglycerides are made from a - reaction between 1 - molecule and 3 - molecules

A

condensation, glycerol, fatty acid

180
Q

triglycerides are more/ less dense than water

181
Q

are triglycerides polar?

A

no they are non-polar

182
Q

because triglycerides are non polar, they are - and -

A

hydrophobic and insoluble

183
Q

glycerol is a simple molecule made from - joined to -

A

3 carbon atoms, 3 hydroxyl groups

184
Q

saturated acids have - double bonds

185
Q

unsaturated acids have - double bonds

186
Q

fatty acids contain an acidic - group

A

carboxyl group

187
Q

fatty acids carboxyl group

188
Q

fatty acids have a general formula of - where R is a -

A

R.COOH, hydrocarbon tail

189
Q

most naturally occurring fatty acids have - to - carbon atoms

190
Q

phospholipids are produced when

A

an OH group of the glycerol combines with a phosphoric acids

191
Q

phospholipids have a - head with 2 - tails

A

phosphate, fatty acid hydrocarbon

192
Q

in phospholipids the fatty acid chains are -

A

hydrophobic

193
Q

in phospholipids the phosphate head is - and -

A

polar and hydrophilic

194
Q

cholesterol is made of - - rings

195
Q

cholesterol is found in all …

A

biological membranes

196
Q

cholesterol is - and -

A

small and hydrophobic

197
Q

cholesterol is made in the

198
Q

which type of fatty acid can bend

A

unsaturated

199
Q

which type of fatty acid melts at a higher temperature

200
Q

which type of fatty acid is solid at room temperature

201
Q

excess cholesterol clumps in bile to form

A

gall stones

202
Q

what is familial hypercholesterolemia?

A

a genetic disorder where the signal to stop cholesterol production fails, causing heart attacks at very young ages

203
Q

how do you test for lipids

A

emulsion test

  1. mix sample with ethanol
  2. add solution to water
  3. shake
204
Q

if lipids are present, the emulsion test will show

A

a white emulsion layer formed at the top

205
Q

to make the emulsion test semi quantitative, we can…

A

measure the density of a well mixed sample in a colorimeter

206
Q

what are bisensors

A

an analytical device for the quantitative measurement of a biological response

207
Q

ca2+ role

A

bone structure, muscle contraction, amylase cofactor, synaptic transmission

208
Q

is anion positive or negative

209
Q

is cation positive or negative

210
Q

na+ role

A

nerve transmission, in LOH/CD, counter current multiplier

211
Q

k+ role

A

nerve transmission, guard cell opening

212
Q

h+ role

A

H bonds, blood pH, ETC in respiration

213
Q

NH+4 role

A

formed from deamination of amino acids

214
Q

NO-3 role

A

N source for plants to build up amino acids

215
Q

HCO-3 role

A

CO2 transport, plasma buffer

216
Q

Cl- role

A

amylase cofactor

217
Q

PO-3,4 role

A

in phospholipids, ATP and nucleic acids

218
Q

OH- role

A

involved in bonds

219
Q

TESTING FOR REDUCING SUGARS qualitative method

A
  1. add 10cm3 of benedicts to sample
  2. place in 100 degrees c water bath for 15 mins
  3. goes from blue- brick red if sugars present
220
Q

TESTING FOR NON-REDUCING SUGARS qualitative method

A
  1. hydrolyse the sugar in acid
  2. add 10cm3 of benedicts to sample
  3. place in 100 degrees c water bath for 15 mins
  4. goes from blue- brick red if sugars present
221
Q

TESTING FOR REDUCING SUGARS quantitative method

A
  1. create glucose dilution series of 1%, 0.5%, 0.25%, 0.13%, 0.06% and UNKNOWN in beakers
  2. place 2cm3 in boiling tubes
  3. add 10cm3 of benedicts
  4. place in 100 degrees c water bath for 15 mins
  5. place in centrifuge tubes and centrifuge for 2 mins each
  6. take supernatant and pipette into cuvettes
  7. calibrate colorimeter with water in cuvette, should read 100% (red, transmission)
  8. put cuvettes into colorimeter and record readings
  9. create calibration curve on graph paper and use to determine unknown glucose concentration.

biology module 2- foundations in biology (6 decks)

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