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AH Biology > 1.2 Proteins > Flashcards

1.2 Proteins Flashcards

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1
Q

The proteome

A

The entire set of proteins expressed by a genome

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2
Q

The entire set of proteins expressed by a genome

A

Proteome

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3
Q

Compare the size of proteome to the genome

A

Proteome is much larger than the genome

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4
Q

Why is the proteome larger than the genome

A

As more than one protein can be expressed from a single gene due to alternative RNA splicing

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5
Q

Alternative RNA splicing

A

Different combinations of exons will be spliced together

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6
Q

What does alternative splicing mean for the preteome

A

It is much larger

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7
Q

Different combinations of exons will be spliced together

A

Alternative RNA splicing

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8
Q

Genome -> _______ -> proteome

A

Alternative RNA splicing

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9
Q

Genome -> alternative RNA splicing -> _______

A

Proteome

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10
Q

_____ -> alternative RNA splicing -> proteome

A

Genome

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11
Q

Transcriptome

A

The full range of mRNA transcript

Includes primary and mature

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12
Q

The full range of mRNA transcript

Includes primary and mature

A

Transcriptome

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13
Q

Compare the size of the transcriptome to genome

A

transcriptome is bigger due to alternative RNA splicing

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14
Q

Compare the size of the transcriptome to the proteome

A

transcriptome Is smaller than the proteome due to post translational modification

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15
Q

Why are not all genes expressed by all cell types

A

Metabolic activity

State of cellular stress

Response to signalling molecules

State of health and disease

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16
Q

Due to their _____ size, eukaryotic cells have a relatively small surface area to volume ratio

A

Large

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17
Q

Due to their large size, eukaryotic cells have a relatively _____ surface area to volume ratio

A

Small

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18
Q

What do eukaryotic cells have to increase surface area

A

An internal system of specialised membranes, the ER

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19
Q

Purpose of the internal system of specialised membranes, the ER eukaryotic cells have

A

To increase surface area

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20
Q

What does the ER form

A

A network of membrane tubules continuous with the nuclear membrane

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21
Q

What form a network of membrane tubules continuous with the nuclear membrane

A

The ER

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22
Q

Categories of ER

A

Rough

Smooth

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23
Q

ER

A

endoplasmic rectilum

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24
Q

Rough endoplasmic rectilum ribosomes

A

Has docked ribosomes on its cytosolic face

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25
Q

Has docked ribosomes on its cytosolic face

A

Rough ER

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26
Q

Smooth ER ribosomes

A

Lacks ribosomes

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27
Q

Lacks ribosomes

A

Smooth ER

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28
Q

Golgi apparatus

A

A series of flattened membrane discs that has associated vesicles to transport materials between component parts

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29
Q

A series of flattened membrane discs that has associated vesicles to transport materials between component parts

A

Golgi apparatus

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30
Q

Lysosomes

A

Formed from specialised Golgi vesicles, they are membrane bound organelles containing of variety of hydrolyses

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31
Q

Formed from specialised Golgi vesicles, they are membrane bound organelles containing of variety of hydrolyses

A

Lysosomes

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32
Q

Hydrolases

A

Enzymes that digest proteins, lipids, nucleic acids, and carbohydrates

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33
Q

Enzymes that digest proteins, lipids, nucleic acids, and carbohydrates

A

Hydrolases

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34
Q

Main components in the membrane

A

Proteins

Phospholipids

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35
Q

Proteins and phospholipids

A

Formed into a bilayer and have a hydrophilic head and hydrophobic tail

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36
Q

Formed into a bilayer and have a hydrophilic head and hydrophobic tail

A

Lipids

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37
Q

Where are lipids synthesised

A

The SER

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38
Q

What are synthesised in the SER

A

Lipids

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39
Q

What happens to lipids after being synthesised

A

Inserted into the membrane of the SER

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40
Q

What begins at the cytosolic ribosomes

A

The synthesis of all proteins

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41
Q

Where does the synthesis of all proteins begin

A

The cytosolic ribosomes

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42
Q

Where is the synthesis of cytosolic proteins completed

A

At the cytosolic ribosomes

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43
Q

What happens once cytosolic proteins are synthesised

A

They remain in the cytoplasm where they carry out their specialised function

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44
Q

what remain in the cytoplasm where they carry out their specialised function after being synthesised

A

Cytosolic proteins

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45
Q

What do transmembrane proteins carry

A

A signal sequence

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46
Q

A signal sequence

A

A short stretch of 16-30 amino acids at one end of the polypeptide that will determine the eventual location of that protein in a cell

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47
Q

A short stretch of 16-30 amino acids at one end of the polypeptide that will determine the eventual location of that protein in a cell

A

Signal sequence

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48
Q

Where are transmembrane proteins attached

A

The membrane

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49
Q

Synthesis is of transmembrane proteins
(3)

A

The synthesis of transmembrane proteins begin in the cytosolic ribosomes

Synthesis is completed when the signal sequence halts translation and the relevant cytosolic ribosomes dock with the ER and become part of the RER

After docking, the signal sequence is removed and the protein is inserted into the ER.

Once proteins are in the ER membrane, they are transported in the membrane of vesicles that bud off from the ER and fuse with the Golgi

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50
Q

The synthesis of transmembrane proteins begin in the cytosolic ribosomes

Synthesis is completed when the signal sequence halts translation and the relevant cytosolic ribosomes dock with the ER and become part of the RER

After docking, the signal sequence is removed and the protein is inserted into the ER.

Once proteins are in the ER membrane, they are transported in the membrane of vesicles that bud off from the ER and fuse with the Golgi

A

Synthesis of transmembrane proteins

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51
Q

Movement of proteins between intercellular membranes

A

Once the proteins are in the ER, they are transported by vesicles that bud off from the ER and fuse with the Golgi apparatus

As proteins move through the Golgi apparatus they undergo post-translational modification

The addition of carbohydrate groups is the major modification

Vesicles that leave the Golgi apparatus take proteins to the plasma membrane and lysosomes

Vesicles move along microtubules to other membranes and fuse with them within the cell

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52
Q

Once the proteins are in the ER, they are transported by vesicles that bud off from the ER and fuse with the Golgi apparatus

As proteins move through the Golgi apparatus they undergo post-translational modification

The addition of carbohydrate groups is the major modification

Vesicles that leave the Golgi apparatus take proteins to the plasma membrane and lysosomes

Vesicles move along microtubules to other membranes and fuse with them within the cell

A

Movement of proteins between intercellular membranes

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53
Q

The secretory pathway

A

Secreted proteins are translated in ribosomes on the RER and enter its lumen

The proteins move through the Golgi apparatus and are then packaged into secretory vesicles

These vesicles move to and fuse with the plasma membrane, releasing the proteins out of the cell

Many secreted proteins are synthesised as inactive precursors and require proteolytic cleavage to produce active protein

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54
Q

Secreted proteins are translated in ribosomes on the RER and enter its lumen

The proteins move through the Golgi apparatus and are then packaged into secretory vesicles

These vesicles move to and fuse with the plasma membrane, releasing the proteins out of the cell

Many secreted proteins are synthesised as inactive precursors and require proteolytic cleavage to produce active protein

A

Secretory pathway

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55
Q

Order of secretory pathway

A

RER→ GA → Secretory vesicles→ plasma membranes→ extracellular space

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56
Q

What elements are in amino acids

A

C
O
N
H

Sometimes S

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57
Q

Amino acids have different/the same structure

A

The same

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58
Q

What differs between amino acids

A

R groups

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59
Q

Four groups of amino acids

A

Non polar

Polar

Acidic

Basic

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60
Q

Non polar

Polar

Acidic

Basic

A

Groups of amino acids

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61
Q

Non polar characteristic

A

Hydrophobic

Purely CH

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62
Q

Hydrophobic is polar/non polar

A

Non polar

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63
Q

polar characteristic

A

Hydrophilic

Presence of O

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64
Q

Hydrophilic

Presence of O

A

Polar

65
Q

Acidic characteristic

A

Negatively charged

66
Q

Negatively charged

A

Acidic

67
Q

Basic characteristic

A

Positively charged

68
Q

Positively charged

A

Basic

69
Q

4 levels of protein structure

A

Primary

Secondary

Tertiary

Quarternary

70
Q

Primary

Secondary

Tertiary

Quarternary

A

4 levels of protein structure

71
Q

Amino acid sequence determines what

A

Protein structure

72
Q

Proteins are what of amino acids

A

Polymers

73
Q

What are amino acids linked by

A

Peptide bonds

74
Q

What do amino acids linked by peptide bonds form

A

Polypeptide

75
Q

Peptide bonds formula

A

CONH

76
Q

How are the groups an amino acids in determined

A

By their R group

77
Q

The wide range of functions carried out by proteins results from what

A

The diversity of R groups

78
Q

Primary structure of proteins

A

The sequence in which the amino acids are synthesised into the polypeptide

79
Q

The sequence in which the amino acids are synthesised into the polypeptide

A

The primary structure of proteins

80
Q

Hydrogen bonding occurs along what on proteins

A

The backbone of the protein strand

81
Q

What occurs along backbone of the protein strand

A

Hydrogen bonding

82
Q

Hydrogen bonding along the backbone of the protein strand results in what

A

Regions of secondary structure

83
Q

what functional groups does an amino acid have

A

amine NH2

carboxyl COOH

84
Q

Types of secondary structure

A

Alpha helices (helix)

Parallel beta pleated sheets

Anti parallel beta pleated sheets

Turns

85
Q

Alpha helices (helix)

Parallel beta pleated sheets

Anti parallel beta pleated sheets

Turns

A

Types of secondary structure

86
Q

What does the protein polypeptide fold into

A

A tertiary structure

87
Q

The tertiary structure of proteins

A

How the polypeptide folds

This confirmation is stabilised by interactions between R groups:

Hydrophobic interactions
Ionic bonds
LDFs
Hydrogen bonds
Disulfide bridges

88
Q

How the polypeptide folds

This confirmation is stabilised by interactions between R groups:

Hydrophobic interactions
Ionic bonds
LDFs
Hydrogen bonds
Disulfide bridges

A

The tertiary structure of proteins

89
Q

Disulfide bridges

A

Covalent bonds between R groups containing sulphur

90
Q

Covalent bonds between R groups containing sulphur

A

Disulfide bridges

91
Q

What does quaternary structure of proteins exist in

A

Proteins with two or more connected polypeptide subunits

92
Q

What exists between proteins with two or more connected polypeptide subunits

A

Quaternary structure

93
Q

What does quarternary structure describe

A

The spatial arrangement of the subunits

94
Q

What describes the spatial arrangement of the subunits

A

Qarternary structure

95
Q

What proteins commonly require proteolytic cleavage

A

Digestive enzymes

96
Q

Prosthetic group

A

A non protein unit tightly bound to a protein and necessary for its function

97
Q

A non protein unit tightly bound to a protein and necessary for its function

A

Prosthetic group

98
Q

The ability of haemoglobin to bind oxygen is dependent on what

A

The protein haem group

99
Q

What depends on the protein haem group

A

The ability of haemoglobin to bind oxygen

100
Q

What can interactions of the R groups be influenced by

A

Temperature and pH

101
Q

Increasing temperature effect on protein

A

Disrupts the interactions that hold the protein in shape

The protein begins to unfold and eventually becomes denatured

102
Q

Disrupts the interactions that hold the protein in shape

The protein begins to unfold and eventually becomes denatured

A

Increasing temperature on protein

103
Q

What affects the charges on acidic and basic R groups

A

pH

104
Q

Effect of pH increasing or decreasing from optimum pH on protein

A

The normal ionic interactions between charged groups are lost

This gradually changes the confirmation of the protein until it becomes denatured

105
Q

The normal ionic interactions between charged groups are lost

This gradually changes the confirmation of the protein until it becomes denatured

A

Effect of increasing or decreasing pH past the optimum on the protein

106
Q

Ligand

A

A substance that can bind to a protein

107
Q

A substance that can bind to a protein

A

Ligand

108
Q

R groups not involved in protein folding can allow what

A

Binding to ligands

109
Q

What can allow binding to ligands

A

R groups not involved in protein folding

110
Q

Bonding sites for ligands have what

A

Complementary shape and chemistry to the ligand

111
Q

Stages of ligand binding to protein

A

Binding site on protein has a complementary chemistry and shape

As the ligand binds to the protein binding site, the conformation of the protein changes

The change in conformation cause a functional change in the protein

112
Q

The change in conformation causes a __________ when a ligand binds to protein

A

Functional change in the protein

113
Q

Allosteric interactions occur between what

A

Spatially distinct sites on proteins

114
Q

What occurs between spatially distinct sites on proteins

A

Allosteric interactions

115
Q

The binding of a substrate molecule to one active site of an allosteric enzyme does what

A

Increases the affinity of the other active sites for binding of subsequent substrate molecules

116
Q

What increases the affinity of the other active sites for binding of subsequent substrate molecules

A

The bonding of a substrate molecule to one active site of an allosteric enzyme

117
Q

Why is the binding of substrate to allosteric enzymes important

A

It had biological importance as the activity of allosteric enzymes can vary greatly with small changes in substrate concentration

118
Q

What has biological importance as the activity of allosteric enzymes can vary greatly with small changes in substrate concentration

A

The binding of a substrate to allosteric enzymes

119
Q

What structure do many allosteric proteins have

A

They have multiple subunits

Quaternary structure

120
Q

Allosteric proteins with multiple subunits show what

A

Cooperativity in binding

Changes in binding at one subunit alter the affinity of the remaining subunits

121
Q

What shows cooperativity in binding

A

Allosteric proteins with multiple subunits

122
Q

Allosteric enzymes contain what

A

A second type of site, called an allosteric site

123
Q

What contain a second type of site, called an allosteric site

A

Allosteric enzymes

124
Q

Modulators function

A

Regulate the activity of the enzyme when they bind to the allosteric site

125
Q

Regulate the activity of the enzyme when they bind to the allosteric site

A

Modulators

126
Q

What happens when modulators bind to allosteric sites

A

The conformation of the enzyme changes

This alters the affinity of the active site for the substrate

127
Q

What alters the conformation of allosteric sites

A

The bonding of a modulator

128
Q

Positive modulator affect

A

Increase the enzyme’s affinity for substrate

129
Q

Increase the enzyme’s affinity for substrate

A

Positive modulator

130
Q

Negative modulator affect

A

Reduces the enzyme’s affinity for the substrate

131
Q

Reduces the enzyme’s affinity for the substrate

A

Negative modulators

132
Q

The binging and release oxygen in haemoglobin shows what

A

Cooperativity

133
Q

Example of cooperativity in allosteric enzymes

A

The binging and release oxygen in haemoglobin

134
Q

Cooperativity in binding of oxygen

A

Changes in binding of oxygen at one subunit alters the affinity of the remaining subunits for oxygen

135
Q

Decrease in pH affect on affinity of haemoglobin for oxygen

A

Lower the affinity

Thus, the binding of oxygen is reduced

136
Q

Increase in temperature affect on affinity of haemoglobin for oxygen

A

Lowers the affinity

Thus, binding of oxygen is reduced

137
Q

What lower the affinity of haemoglobin for oxygen

Thus, binding of oxygen is reduced

A

Reduced pH and temperature increase

138
Q

Reduced pH and increased temperature in actively respiring tissues will do what

A

Reduce the binding of oxygen to haemoglobin and therefore promoting increased oxygen delivery to tissue

139
Q

What reduces the binding of oxygen to haemoglobin and therefore promoting increased oxygen delivery to tissue

A

Reduced pH and increased temperature in actively respiring tissue

140
Q

The addition of removal of phosphate can cause what

A

Reversible conformational change in proteins

141
Q

What can cause reversible conformational change in proteins

A

The addition or removal of phosphate

142
Q

What is the addition or removal of phosphate

A

A common form of post translational modification

143
Q

Protein kinases

A

Catalyse the transfer of a phosphate group to other proteins

144
Q

Catalyse the transfer of a phosphate group to other proteins

A

Protein kinases

145
Q

Protein kinases reaction

A

The terminal phosphate of ATP is transferred to specific R groups

146
Q

The terminal phosphate of ATP is transferred to specific R groups

A

Protein kinases

147
Q

Protein phosphatases

A

Catalyse the reverse reaction of protein kinases

148
Q

Catalyse the reverse reaction of protein kinases

A

Protein phosphatases

149
Q

Phosphorylation brings about what

A

Conformational changes which can affect a proteins activity

150
Q

What brings about conformational changes which can affect a proteins activity

A

Phosphorylation

151
Q

The activity of what are regulated with phosphorylation

A

Many cellular proteins, such as enzymes and receptors

152
Q

What are many cellular proteins, such as enzymes and receptors regulated by

A

Phosphorylation

153
Q

Some proteins are ______ by phosphorylation while others are ______

A

Activated

Inhibited

154
Q

Some _____ are activated by phosphorylation while others are inhibited

A

Proteins

155
Q

Some proteins are activated by _________ while others are inhibited

A

Phosphorylation

156
Q

Adding a phosphate groups adds what

A

Negative charges

157
Q

The addition of what adds negative charges

A

Phosphate groups

158
Q

Result of adding a phosphate group on bond interactions

A

Ionic interactions in the unphosphorylated protein can be disrupted and new ones created

159
Q

What causes ionic interactions in the unphosphorylated protein can be disrupted and new ones created

A

Adding phosphate groups

AH Biology (9 decks)

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