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Biological Molecules Flashcards

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1
Q

What is a polymer

A

Monomers joined to make a larger molecules

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2
Q

What is an example of a polysaccharide

A

Starch

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3
Q

What is a condensation reaction

A

Joins two molecules together with formation of chemical bond, involves elimination of water molecule (polymerisation)

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4
Q

What is a hydrolysis reaction

A

Breaks the chemical bond between two molecules, involves the use of water molecule

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5
Q

What are organic molecules how do they form sequences

A

They contain carbon molecules
Carbon atoms very readily form bonds with other carbon atoms, allowing a sequence of carbon atoms of various lengths to join

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6
Q

What are carbohydrates

A

Hydrated carbons in a 2:1 ratio of carbon and hydrogen:oxygen

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7
Q

What is a saccharide

A

Basic monomer sugar unit in carbohydrates

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8
Q

What is a monosaccharide and the general formula

A 
Sweet tasting soluble substances
General formula (CH2O)n (n can be 3-7)
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9
Q

What are the two isomers of glucose

A

Alpha glucose

Beta glucose

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10
Q

How are reducing sugars tested for (all monosaccharides and some disaccharides)

A

Benedicts test

  1. Add 2cm^3 of food sample to test tube (grind up in water is isn’t already liquid)
  2. Add equal volume of Benedicts reagent
  3. Heat mixture by boiling gently in water bath for 5 minutes
  4. Positive result of reducing sugar seen of solution turns brick red
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11
Q

What type of test is the Benedicts test and how accurate is it

A

Semi-quantitive, estimates the approximate amount of reducing sugar in sample depends on colour solution turns

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12
Q

What is a reducing sugar

A

Can donate electrons to reduce another chemical

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13
Q

What is the colour change in the Benedicts test due to

A

Increasing copper (|) precipitate

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14
Q

Instead of looking at the colour change in the Benedicts test what is another method of testing for a reducing sugar

A

Measure the mass of the reducing sugar, will tell us if more reducing sugar in glucose. Heavier precipitate, more reducing sugar present

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15
Q

What do monosaccharides form after condensation reaction

A

Disaccharide

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16
Q

What disaccharide is formed from the condensation of alpha glucose and alpha glucose

A

Maltose

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17
Q

What disaccharide is formed from the condensation of alpha glucose and fructose

A

Sucrose

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18
Q

What disaccharide is formed from the condensation of alpha glucose and galactose

A

Lactose

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19
Q

What bond is formed between monosaccharides in a condensation reaction to form disaccharides

A

Glycosidic bond

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20
Q

How would you test for a non-reducing sugar

A
  1. Perform Benedicts test with unknown sample, no change, know isn’t reducing sugar
  2. Add 2cm^3 of sample to dilute hydrochloric acid
  3. Heat in boiling water for 5 minutes (hydrolyse the disaccharide into monosaccharides)
  4. Add sodium hydrogen-carbonate solution to neutralise the acid (or would stop Benedicts test working)
  5. Check with pH paper that solution is neutral
  6. Perform Benedicts test, heat
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21
Q

How do you test for starch

A
  1. Add iodine solution, shake

2. If present will turn blue/black

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22
Q

What is the structure or starch

A

Chains of alpha glucose monosaccharides linked by glycosidic bonds by condensation
Unbranched chain wound into tight coil making molecule compact

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23
Q

What is the function of starch

A

Energy storage

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24
Q

Where can starch be found

A

In plants as small grains

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25
Q

What are the features of starch

A

Insoluble, doesn’t draw water into cells by osmosis and doesn’t easily diffuse out of cells easily
Compact so lots can be stored in small space

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26
Q

What happens to starch when it is hydrolysed and why is this good

A

Forms alpha glucose
Easily transported
Readily used in respiration

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27
Q

What is the structure of glycogen

A

Similar to starch but shorter chains of alpha glucose and is much more branched

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28
Q

What is the function of glycogen

A

Major carbohydrate storage product of animals (energy storage)

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29
Q

How is glycogen stored in animals

A

Small granules, mainly in muscles and liver

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30
Q

Why does the structure of glycogen suit it and how does it’s chain length affect hydrolysis

A

Good for energy storage

Made of smaller chains so even more readily hydrolysed to alpha glucose used in respiration

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31
Q

What is the structure of cellulose

A

Made of beta glucose chains (linked by glycosidic binds formed in condensation)
Beta glucose must rotate 180 degrees to neighbour to form glycosidic bonds
So CH2OH group on each beta glucose alternates above and below chain
Straight unbranched chain run parallel allowing H-bonds form cross-linkages between adjacent chains

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32
Q

What is the function of cellulose

A

Major plant cell wall component, provides strength support and rigidity
Prevents cell bursting when water enters - osmosis, it exerts inward pressure, prevent further water entry
Cell can be turgid, help plant semi-rigid, upright (important for photosynthesis)

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33
Q

Why are the cross links important in cellulose and what bond are they made of

A

Hydrogen bonds form between straight unbranched cellulose chains to increase strength and rigidity

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34
Q

What do groups of cellulose molecules form

A

Microfibrils which in turn are arranged in parallel groups to make fibres

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35
Q

What is a lipid made of

A

Carbon, hydrogen and oxygen

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36
Q

What can lipids dissolve in

A

Insoluble in water

Soluble in organic solvents e.g alcohol

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37
Q

What is the main lipid groups

A

Triglycerides and phospholipids

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38
Q

What state are fats and oils at room temperature

A

Fats are solid

Oils are liquid

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39
Q

What are the features of lipids

A

Energy source - when oxidised lipids provide ,ore than twice the energy as same mass of carbohydrate, release valuable water
Waterproofing - insoluble in water. Plants and insects have waxy lipid cuticles, conserve water. Mammals make oily secretion from sebaceous glands
Insulation - fats are slow conductors of heat. Electrical conductors in myelin sheath round nerve cells
Protection - fat often stored around delicate organs e.g kidneys

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40
Q

What is the function of lipids in the cell membrane

A

Phospholipids contribute to membrane flexibility, transfer of lipid soluble substances across them

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41
Q

What is a monomer and examples

A

A smaller unit

Monosaccharides, amino acids, nucleotides

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42
Q

What bond is formed in a triglyceride

A

Ester bond

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43
Q

What is an unsaturated fatty acid and what state is it likely to be

A

Has double carbon bonds, making it more likely to be a liquid as is weaker

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44
Q

Why are triglycerides suited to energy storage role

A

High ratio of energy-storing carbon-hydrogen bonds to carbon atoms, good energy source
Low mass to energy ratio, good storage molecules as much energy can be stored in small volume (good for large animals reduces movement)
Is a large non-polar molecule, insoluble in water so storage doesn’t effect osmosis/water potential of cell
High hydrogen:oxygen atoms, triglycerides release water when oxidised, provide water source

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45
Q

How is a glycolipid formed

A

When phosphate is removed and replaced with a carbohydrate group

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46
Q

Where are glycolipids often found and why are they important

A

Found within cell surface membrane

Important to cells as involved in cell recognition

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47
Q

How are lipids tested for

A

Emulsion test

  1. Dry grease free test tube
  2. Add 2cm^3 sample being tested
  3. Add 5cm^3 ethanol
  4. Shake tube to dissolve any lipid
  5. Add 5cm^3 water, gently shake
  6. Cloudy white emulsion indicated lipid presence
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48
Q

Why does a lipid form a cloudy white emulsion

A

Tiny droplets dispersed in water form emulsion. Light passing through refracted as passes from oil to water droplets

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49
Q

How could you check the emulsion test wasn’t false positive

A

Control could use a non fatty substance e.g water and compare to sample

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50
Q

Why are enzymes important

A

Involved in almost every living process

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51
Q

What is an amino acid made of

A

Has a central carbon atom
NH2- on left of middle carbon
-COOH- acid group on right of middle carbon
R group above (determines the amino acid)
H below

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52
Q

How many amino acids are there

A

20 amino acid groups

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53
Q

What bond forms between two amino acids to make a dipeptide

A

Peptide bond

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54
Q

What is the process when amino acid monomers join

A

Polymerisation

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55
Q

How do you test for a protein

A

Biuret test

  1. Add equal volume of Biuret solution (sodium hydroxide and copper sulphate) to sample
  2. Purple colour indicated peptide bonds presence, so a protein
  3. If no protein remains blue
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56
Q

What is the primary structure of a protein

A

Order of amino acids in polypeptide
Dictated by DNA sequence of gene
Mutations can cause tiny changes, a,y have huge consequences e.g sickle cell
Peptide bonds

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57
Q

What is the secondary structure of a protein

A

Polypeptide chains fold and coils into secondary structure - alpha helix, beta sheet, beta turn
Held by hydrogen bonds between C=O groups of peptide bond

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58
Q

What is the tertiary structure in proteins

A

Alpha helices can be twisted, folded form complex, specific 3D structure
Disulphide bridges between sulphur in R groups
Ionic bonds formed between any carboxyl and amino acid not involved in peptide bonds
Hydrogen bonds easily broken between R groups

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59
Q

What is the quaternary structure of proteins

A

Some proteins have several subunits, two+ peptide chains attached
Some proteins have non-protein ‘prosthetic group’ attached
Has more than one polypeptide chain

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60
Q

What is the role of fibrous proteins and example

A

Structural functions

Collagen

61
Q

What is the function of a globular protein and example

A

Carry out metabolic functions

Enzymes, haemoglobin

62
Q

What is the structure of fibrous proteins

A

Form long parallel chains linked by cross bridges, form very stable molecules
Primary - unbranched polypeptide chain
Secondary - polypeptide chain very tightly wound
Tertiary - twisted into secondary helix
Quaternary - made of three wound polypeptide chains wound together

63
Q

Where is collagen found why is it needed there

A

Tendons, join muscles to bones
Muscles contracts, bone pulled in contraction direction
Individual collagen polypeptide chains in fibres held by bonds between amino acids of adjacent cells

64
Q

Why are cross-linkages between amino acids in collagen important

A

Cross-linkages between amino acids in polypeptide chains prevent individual polypeptide chains sliding past each other, gain strentgh as act as single unit

65
Q

What type of protein is an enzyme

A

Globular

66
Q

What is an enzyme

A

A catalyst

67
Q

What does a catalyst do

A

Alters the speed of chemical reaction without undergoing permanent changes
Speed up biological reactions, so can happen at body temperature

68
Q

Where do enzymes catalyse reactions

A

Inside cells - intracellular

Outside cells - extracellular

69
Q

What causes enzymes to be specific

A

Globular protein has specific tertiary structure hence 3D shape so is specific to catalyse one reaction

70
Q

What is the induced fit

A 
The shape of active site and substrate molecule are complementary 
Like glove (active site) and hand (substrate) both change shape slightly as bind
71
Q

What is activation energy

A

Energy needed to start reaction - break chemical bonds in substance

72
Q

How is activation energy lowered

A

When enzyme-substrate complex formed, as shale changes, enzyme puts strain on substrate molecule. Distorts bonds in substrate, lowers activation energy needed to break bond

73
Q

How do you work out the gradient of a graph

A

Draw a tangent and workout y/x

74
Q

How does temperature effect reactions

A

Increase in kinetic energy of molecules, move more rapidly collide more

75
Q

What happens when an enzyme is denatured

A

Temperature rises causes hydrogen bonds in enzyme to break so active site is no longer complementary to specific substrate and it becomes permanently denatured

76
Q

How do you workout pH

A

-log10[?]

77
Q

What happens to the enzyme is there is extreme pH change

A

Denatured

78
Q

How does pH change alter enzyme active site

A

Changes amino acid charges that form active site so substrate can’t fit

79
Q

How is the active site arrangement partially determined

A

-NH2 and COOH groups of polypeptide making up enzyme, disrupted by hydrogen ions

80
Q

What is a competitive inhibitor

A

Bind to active site, but is not substrate just has a similar molecular shape so complementary, prevents enzyme-substrate complexes forming
Enzyme activity determined by concentration of substrate and inhibitor

81
Q

What is a non-competitive inhibitor

A

Bind to enzyme at site other than active site, alters the active site in doing so. Substrate no longer complementary
Inhibitor and substrate not competing, increasing substrate doesn’t decrease the inhibitor effect

82
Q

What is the metabolic pathway

A

Series of reactions, each step catalysed by enzyme

83
Q

How does the metabolic pathway work

A

Enzymes control metabolic pathway often attached to membrane of cell organelle in very precise sequence
In organelle optimum conditions for enzymes, keep steady concentration of chemical in cell, same chemical often acts as inhibitor of enzyme at reaction start
End product inhibits first enzyme, if concentration of end products increases over normal, more inhibition of the first enzyme, less product made, concentration returns to normal

84
Q

What is DNA and what does it carry

A

Deoxyribosenucleic acid
Carries genetic information
Code that determines the amino acid sequence in protein (primary structure) determines how polypeptide folds up to form precise tertiary structure for protein

85
Q

What is DNA made of

A

Two interlocking nucleotide chains

Nitrogen-containing organic molecules combine form polynucleotide (3+ nucleotides)

86
Q

What is a single nucleotide

A

Monomer or mono-nucleotide

87
Q

How is a nucleotide formed and what is it made of

A

Pentose sugar, phosphate group, organic bases joined by condensation reactions

88
Q

What bond is formed between nucleotide of one group and sugar of another nucleotide, what does it form

A

Phosphodiester bond

Forms sugar-phosphate backbone

89
Q

Who contributed to DNA structure work

A

1953 Watson and Crick published first DNA structure description following Franklins X-ray diffraction DNA patterns work

90
Q

Which are the single-ring bases

A

Cytosine and thymine

91
Q

Which are the double ring bases

A

Adenine and guanine

92
Q

How many hydrogen bonds are between A-T base pairing

A

2

93
Q

How many hydrogen bonds are between C-G base pairing

A

3

94
Q

How are polynucleotides placed

A

Polynucleotide chains are antiparallel run in opposite directions

95
Q

Why is DNA stable

A

Phosphodiester backbone protects more chemically reactive organic bases
Hydrogen bonds link base pairs forming bridges. As C-G have 3 hydrogen bonds more of these pairs make molecule more stable
Single H-bond not string, as many more stable

96
Q

What are the functions of DNA

A

Separate strands joined by H-binds, easily broken allow strands separate for replication
Very large, lots genetic information to be stored
Very stable, passed from generations (rarely mutates)
Bases protected by sugar phosphate backbone prevents corruption by outside chemical/physical forces
Sequence bases codes for primary protein structure
Base pairing lets DNA replicate transfer information to mRNA

97
Q

What is RNA

A

Ribonucleic acid

Single, quite short polynucleotide chain, peptide sugar is ribose and organic bases

98
Q

What is the different base in mRNA

A

Uracil instead of thymine

99
Q

What types of cell division are there

A

Nuclear division

Cytokinesis

100
Q

What occurs in nuclear division

A

Process nucleus divides

Two nuclear division types, mitosis, meiosis

101
Q

What occurs in cytokinesis

A

Follows nuclear division process where whole cell divides

102
Q

What must happen before nucleus divides

A

DNA must be replicated to ensure all daughter cells have genetic information to make enzymes and proteins they need

103
Q

What does semi-conservative replication need

A

Four nucleotide types with A,C,G,T bases
Both DNA molecule strands acts as template for nucleotide attachment
Enzymes DNA helicase and RNA polymerase
Chemical energy source to drive process

104
Q

What are the stages in the semi-conservative process

A
  1. Representative portion of DNA undergo replication
  2. Enzyme DNA helicase causes 2 DNA strands to separate, strands unwind breaking hydrogen bonds that join complementary bases
  3. Once activated nucleotides bound, joined by RNA polymerase in condensation reactions form phosphodiester bonds. Remaining free bases attract to complementary nucleotides
  4. All nucleotides joined form complete polynucleotide chain using RNA polymerase. Two identical strands of DNA, one original one new in each
105
Q

What were the hypotheses of Watson and Crick

A

Conservative model and the semi-conservative model for DNA replication

106
Q

What did the conservative model suggest

A

Originality DNA molecule remained intact, separate daughter DNA copy built from new molecules of deoxyribose, phosphate, organic bases. One entirely new material, one entirely original material

107
Q

What did the semi-conservative model suggest

A

Original DNA molecule slips into two separate strands, each replicated its mirror image
Two new molecules would have one new material and one original material in one strand

108
Q

What facts did Meselsohn and Stahl base their work to test the (semi)conservative models on

A

All DNA bases contain nitrogen
Nitrogen has two forms, N14 lighter than N15
Bacteria will incorporate nitrogen from growing medium into any new DNA made

109
Q

How Meslsohn and Stahl test the (semi)conservative model

A

Labelled original DNA of bacteria by growing N15 medium
Transferred bacteria to medium of N14, single generation to replicate once
Mass of each ‘new’ DNA depend on which replication method occurred
Centrifuge extracted DNA
Lighter DNA nearer top of tube would be collected
Analyse DNA after 2 then 3 generations
Interpret results, determine which hypothesis correct

110
Q

What is ATP made of and what does it do

A 
A phosphorylated macromolecule
Adenine nitrogen-containing organic base
Ribose sugar molecule, 5-carbon ring structure (pentose sugar) acts as backbone where other parts attach 
Phosphates, chain of 3 phosphate groups 
Stores ATP's energy
111
Q

When is energy released due to phosphate groups

A

Bonds between phosphate groups unstable, lower activation energy so easily broken. When break energy released

112
Q

What is the reaction equation of ATP releasing energy

A

ATP+(H2O)->ADP+Pi+E

E = energy - ATPase

113
Q

Why is water in the reaction of ATP forming ADP

A

Hydrolysis reaction, catalysed by enzyme ATP hydrolase

114
Q

What type of reaction is ATP forming ADP

A

Reversible reaction , energy can be used to add inorganic phosphate to ADP, reform ATP according to reverse of equation
Reaction catalysed by enzyme ATP synthase in condensation reaction

115
Q

What ways does ATP synthesis occur to add a phosphate to ADP

A

In chlorophyll - containing plant cells during photosynthesis (photophosphorylation)
In plant, animal cells in respiration (oxidative phosphorylation)
In plant, animal cells when phosphate groups transferred from donor molecules to ADP (substrate-level phosphorylation)

116
Q

What make ATP a good energy donor

A

Instability of phosphate bonds

ATP is an immediate energy source of a cell

117
Q

What makes ATP not a good long term energy store, what are better stores

A

Instability of phosphate bonds

Fats and carbohydrates e.g glycogen

118
Q

Why is ATP a better immediate energy source than glucose

A

Release less energy than each glucose molecule. Energy for reactions released in smaller, manageable quantities
Hydrolysis of ATP to ADP is single reaction that releases immediate energy

119
Q

Where is ATP made

A

ATP cant be stored has to continuously be made in mitochondria of cells that need energy e.g muscle fibres

120
Q

Which processes in cells is ATP used

A 
Metabolic processes
Movement 
Active transport 
Secretion 
Activation of molecules
121
Q

Why is ATP needed in metabolic processes

A

Provides energy needed to build up macromolecule from basic units e.g making starch from glucose

122
Q

Why is ATP needed in movement

A

Provides energy for muscle contraction. In muscle contraction ATP provides energy for muscle filaments to slide past each other, often shorter muscle fibre length

123
Q

Why is ATP needed in active transport

A

Energy to change carrier protein shape in plasma membranes lets molecules/ions move against concentration gradient

124
Q

Why is ATP needed in secretion

A

To form lysosomes needed for cell product secretion

125
Q

Why is ATP needed in activation of molecules

A

In organic phosphate released during ATP hydrolysis, can be used to phosphorylate other compounds to make them more reactive, lower activation energy in enzyme-catalysed reaction

126
Q

What charge does a water molecule have

A

No overall charge
Oxygen slightly negative
Hydrogen slightly positive
Is dipolar due to positive and negative poles

127
Q

What is the attractive force between opposite charges

A

Hydrogen bond
Each bond fairly weak
Form important forces cause water molecules stick together, has unusual properties

128
Q

Why does water have a high specific heat capacity

A

The molecules stick together so more energy (heat) needed to separate them than if didn’t bond together

129
Q

Why is it good that water has a high specific heat capacity

A

Acts as a buffer against sudden temperature variations, aquatic environment is stable temperature

130
Q

Why does water have a high latent heat

A

Hydrogen bonding between molecules mean lots of energy to evaporate 1 gram of water

131
Q

How do mammals body cool itself effectively

A

Evaporation of water (sweat) from skin

132
Q

What is cohesion

A

Tendency of molecules to stick together. Hydrogen bonding, water has large cohesive forces, allow it to be pulled up through a tube e.g xylem vessel
Force is surface tension so water surface acts like skin, strong enough to support small organisms

133
Q

Why is water an important molecule in reactions within the body

A

Breaks down many complex molecules by hydrolysis and produced in condensation reactions

134
Q

What medium does chemical reactions occur in

A

Aqueous medium

135
Q

What substances does water dissolve

A

Gases
Wastes e.g amino acids
Inorganic ions and small hydrophilic molecules e.g ATP
Enzymes, whose reactions take place in solution

136
Q

Why is it good that water is not easily compressed

A

Provides support

137
Q

Why is it important water is transparent for plants

A

Transparent, aquatic plants photosynthesise, light rays can penetrate jelly-like fluid

138
Q

What colour light does a plant reflect

A

Green light

139
Q

What happens to water as it freezes why is this beneficial

A

Expands, density decreases so ice less dense than water

Insulates sea underneath

140
Q

What is specific heat capacity

A

Amount of energy needed to raise 1kg of water by 1 degree

141
Q

What is specific latent heat

A

Amount of energy to evaporate 1 gram of water

142
Q

Where are inorganic ions found

A

In organisms where occur in solution in the cytoplasmic the cytoplasm of cells and body fluids and part of larger molecules

143
Q

What do inorganic ions do

A

Range of functions
Specific function a particular ion performs, related to properties e.g iron ions in haemoglobin where play a role in oxygen transport

144
Q

Why are hydrogen ions important

A

They determine solution pH so enzymes functioning

145
Q

What is a cation

A

Positive ion e.g sodium , iron, hydrogen

146
Q

What is an anion

A

Negative ion e.g phosphate

147
Q

What is the function of sodium ions

A

Help glucose, amino acid transport

148
Q

What are iron ions important for

A

Part of haemoglobin

149
Q

Why are phosphate ions important

A

Essential parts of DNA, RNA, ATP

Biology (4 decks)

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