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Cfe Advanced Higher Biology - Unit 1 > 1.2 PROTEINS > Flashcards

1.2 PROTEINS Flashcards

1
Q

What is the Genome?

A

An organism’s complete set of DNA

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2
Q

What is the Proteome?

A

The entire set of proteins expressed by a genome.

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3
Q

Why is the Proteome larger than the Genome?

A

Due to alternative RNA splicing and post-translational modification

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4
Q

What is the result of Gene Expression?

A

Not all genes are expressed as proteins in a particular cell

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5
Q

What is the benefit of Gene Expression?

A

Only essential proteins are produced and therefore the cell is more energy and resource efficient

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6
Q

What does amino acid sequence determine?

A

Protein structure

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7
Q

What is a protein?

A

A polymer of amino acid monomers

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8
Q

Which type of bond links amino acids?

A

Peptide bonds

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9
Q

What is a chain of amino acids called?

A

Polypeptide

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10
Q

What are the four types of protein structure?

A

Primary, Secondary, Tertiary and Quaternary

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11
Q

What is the primary structure of a protein?

A

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

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12
Q

What is the secondary structure of a protein?

A

Alpha helices / Beta sheets / Turns

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13
Q

What causes secondary structure?

A

Hydrogen bonding along the backbone of the protein

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14
Q

What is the tertiary structure of a protein?

A

3D folding of the polypeptide

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15
Q

What causes tertiary structure?

A

Bonding - interactions between R groups, hydrophobic/hydrophilic interactions, ionic bonds, van der Walls interactions, disulfide bridges

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16
Q

What is an R group?

A

Functional group attached to the amino and carboxyl group compound (other component of amino acids). They are the only thing which distinguishes the 20 different amino acids.

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17
Q

What affects R group interactions?

A

Temperature and PH

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18
Q

Other than folding, what else is included in tertiary structure?

A

Prosthetic groups

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19
Q

What are prosthetic groups?

A

Non-protein unit bound to a protein which is essential for protein function

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20
Q

What is the quaternary structure of a protein?

A

Consisting of several connected polypeptide sub-units

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21
Q

What influences the location of proteins in cells?

A

Hydrophobic and Hydrophilic Interactions

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22
Q

What determines the location of proteins in a cell?

A

R groups at the surface of the proteins

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23
Q

What is a soluble protein?

A

A protein found in the cytoplasm

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24
Q

What do Hydrophilic R groups in soluble proteins do?

A

The R groups predominate at the suface of the protein

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25
What does predominate mean?
To become the strongest or main element; greater in number
26
What do Hydrophobic R groups in soluble proteins do?
The R groups may cluster at the centre to form a globular structure
27
What is the name of membrane model we study?
Fluid mosiac model
28
What are the two types of membrane protein?
Integral and peripheral
29
Give an example of an integral membrane protein.
Transmembrane protein (eg. Channel, transporter, receptor)
30
What holds integral proteins within the phospholipid bilayer?
Strong hydrophobic reactions caused by regions of hydrophobic R groups
31
What is the difference between the R groups in peripheral and integral proteins?
Peripheral proteins have fewer hydrphobic R groups interacting with the phospholipids compared to integral proteins
32
What is a ligand?
A substance which can bind to a protein
33
What allows proteins to bind to ligands?
R groups NOT involved in protein folding can allow binding
34
What must ligand-binding sites have?
A complementary shape and chemistry to the ligand
35
What can DNA bind to?
A number of proteins
36
How does DNA bind to histone proteins?
Positively charged histone proteins bind to negatively charged sugar-phosphate DNA backbone in eukaryotic cells
37
What is the benefit of DNA binding to histone proteins?
DNA wraps around histones forming nucleosomes which pack the DNA in chromosomes
38
What do nucleosomes do?
They pack DNA in chromosomes
39
How do proteins (other than histones) bind to DNA?
They have binding sites specific to particular sequences of double-stranded DNA
40
What can proteins (other than histones) do when bound to DNA?
Stimulate or inhibit transcription
41
What is the result of a ligand binding to a protein?
Conformational change of protein
42
What is the result of a substrate binding to an enzyme's active site?
Conformational change of enzyme (protein)
43
What is the result of a conformational change of a protein?
Functional change
44
What is induced fit?
A temporary change in the shape of an enzyme's active site
45
What causes induced fit?
Correct substrate begins to bind to enzyme's active site
46
What is the result of induced fit?
Increases the binding and interaction of the enzyme with the substrate
47
What is activation energy?
The minimum quantity of energy required in order to undergo a particular reaction
48
How do enzymes lower activation energy?
The chemical environment lowers the activation energy required
49
What happens after catalysis?
The original enzyme conformation is resumed and products are released from active site
50
What is an allosteric enzyme?
An enzyme which changes its conformation upon the binding of a modulator to a secondary binding site
51
What are the two types of modulators?
Positive and negative
52
What is the result of a modulator binding to an allosteric enzyme?
Conformational change of enzyme, altering affinity of active site for the substrate
53
What is the result of a positive modulator binding to an allosteric enzyme?
Increases enzyme's affintiy for substrate
54
What is the result of a negative modulator binding to an allosteric enzyme?
Reduces enzyme's affintiy for substrate
55
What is cooperativity?
When the binding of a ligand at one site influences binding at a second site
56
Which type of proteins does cooperativity affect?
Proteins with quaternary structure
57
What is the result of cooperativity in proteins with quaternary structure?
Binding at one subunit alters the affinity of the remaining subunits
58
What is the result of a haemoglobin subunit binding to a molecule of oxygen?
The second subunit binds more easily, the third even more and the fourth easier still
59
What is the result of an oxy-haemoglobin subunit releasing its oxygen?
The second subunit is more likely to release its oxygen and so on.
60
Which factors affect haemoglobin's ability to bind to oxygen?
Temperature and pH
61
How does temperature affect haemoglobin's ability to bind to oxygen?
As temperature increases, affinity for oxygen decreases
62
How does pH affect haemoglobin's ability to bind to oxygen?
As pH decreases, affinity for oxygen also decreases
63
What can be used to cause a reversible conformational change in a protein?
The addition or removal of phosphate from particular R groups
64
What is the addition/removal of phosphate from particular R groups a common form of?
Post-translational modification
65
What is the benefit of a reversible conformational change?
Allows activity of cellular proteins to be regulated
66
What is a kinase enzyme?
An enzyme which catalyses the transfer of a phosphate group from ATP to another molecule
67
What are kinases responsible for?
Phosphorylation of other proteins
68
What are phosphatases responsible for?
They catalyse dephosphorylation
69
What are ATPases responsible for?
Using ATP to catalyse their own phosphorylation
70
What is myosin?
A fibrous protein which forms the contractile filaments of muscle cells
71
What is myosin responsible for?
Muscle contraction
72
What happens when ATP binds to myosin?
Myosin head detaches from actin, swings forwards and rebinds
73
What is the result of myosin rebinding?
ADP and a phosphate ion is released, dragging the myosisn along the actin filament
74
What are the four classes of R groups?
Acidic (Negative), Basic (Positive), Polar, Hydrophobic

Cfe Advanced Higher Biology - Unit 1 (6 decks)

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