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Advanced Higher Biology > Unit 1 - section 2 > Flashcards

Unit 1 - section 2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the proteome?

A

The entire set of proteins expressed by the genome

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2
Q

What is the genome?

A

Entire hereditary information encoded in DNA

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3
Q

2 processes that are responsible for the proteome being much larger than the genome

A

Alternative RNA splicing

Post translational modification

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4
Q

Why is the entire genome not expressed in all cells?

A

Regulation of gene expression

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5
Q

What is the monomer that forms the basic structure of a protein?

A

Amino acids

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6
Q

What is the polymer formed from amino acids?

A

A polypeptide (protein)

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7
Q

What level of protein structure is the polypeptide chain?

A

Primary level

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8
Q

What type of bonds are involved in the basic (primary) structure and how are they formed?

A

Peptide bonds

Formed by dehydration reactions (between a carboxyl group and amide group)

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9
Q

What are the 4 main classes of amino acid side chains (R groups)

A

Acidic
Basic
Polar
Non-polar

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10
Q

For acidic amino acid state:
Examples (2)
Hydrophilic or hydrophobic
Common feature

A

Examples:
Aspartic acid
Glutamic acid

Hydrophilic

Have a carboxyl group which ionises to make them acidic

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11
Q

For basic amino acids state:
Examples (3)
Hydrophilic or hydrophobic
Common feature

A

Examples:
Arginine
Lysine
Histidine

Hydrophilic

Have an additional amino acid group which ionises to NH3^+

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12
Q

For polar amino acids state:
Examples (6)
Hydrophilic or hydrophobic
Common feature

A 
Examples:
Glutamine
Tyrosine
Asparagine
Theonine 
Cysteine 
Serine

Hydrophilic

Different functional groups which contain
-OH, -SH, =O

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13
Q

For non-polar amino acids state:
Examples (9)
Hydrophilic or hydrophobic
Common feature

A 
Examples:
Isoleucine
Tryptophan 
Phenylalanine
Glycine
Methionine 
Alanine
Leucine
Proline
Valine

Hydrophobic

R-group is a hydrocarbon

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14
Q

Name and describe the secondary structures of protein

A

Alpha helix - protein is a helix shape held together by hydrogen bonds between amino acids

Beta sheets - parts of the polypeptide chain run alongside each other to form a corrugated sheet.
Antiparallel beta sheets horizontal hydrogen bonds
Parallel - beta sheets have diagonal hydrogen bonds

Turns - reverses the direction of the polypeptide chain.
Their exact role has not been determined

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15
Q

What bonds are involved in holding the secondary structure of proteins in place

A

Hydrogen bonds

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16
Q

Describe the tertiary structure of proteins using globular proteins as an example

A

The 3D shape of the protein. This further folding is due to the interactions between R-groups

Globular proteins:
Formed due to non polar R-groups clumping together in centre of protein where they are held together by hydrophobic interactions
Amino acids with hydrophobic R-groups usually end up in centre of protein since repelled by water

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17
Q

4 types of bonds that can hold the tertiary structure of proteins in place

A 
Hydrophobic interactions
Ionic bonds
Hydrogen bonds
Van Der Waals interactions
Disulfide bridges
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18
Q

Name the non protein part added to some proteins

A

Prosthetic groups

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19
Q

2 examples of prosthetic groups added to proteins

A

Carbohydrates

Nucleic acid

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20
Q

Give an example of a protein that contains a non-protein group and describe its function

A

Haemoglobin contains prosthetic group haeme and has function of supplying red blood cells with oxygen

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21
Q

Describe the quaternary structure

A

Exists in proteins that have two or more tertiary sub units joined together
Bonding between subunits means that changes to conformational shape of one polypeptide chain can effect the properties of another subunit in the protein

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22
Q

2 factors that can influence the interaction of R groups

A

pH

Temperature

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23
Q

How does
a)pH
b)temperature
Affect R group interactions

A

a) Increase temperature Ek of proteins increases, placing stress on bonds and breaking them. Weaker intermolecular bonds are particularly susceptible

b) Changes pH affect concentration H+ and OH- ions in a solution
Changes the relative charge of protein and places stress in polar interactions such as H bonding and ionic bonding

Changes result denaturation of protein and the loss of tertiary structure and function

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24
Q

Define hydrophobic and hydrophilic

A

Hydrophobic - to repel or fail to mix with water

Hydrophilic- to dissolve or mix with water

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25
Q

What is the current accepted model of the plasma membrane structure?

A

Fluid mosaic model

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26
Q

What are the main components of the plasma membrane?

A

Phospholipids

Proteins

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27
Q

What is the significance of hydrophobic and hydrophilic interactions in membrane structure?

A

Hydrophobic reactions between lupus tails hold the double membrane together
The hydrophilic heads of phospholipids allow the outer layers of the membrane to be surrounded by aqueous solutions

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28
Q

Define the terms integral and peripheral membrane proteins and describe how they are held in position in the membrane?

A

Integral proteins- penetrate the hydrophobic layer of the membrane. They contain a stretch of non-polar amino acids in the hydrophobic region, which holds them in place

Peripheral proteins - not embedded in the lipid layer but have loose associations with the surface of the membrane

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29
Q

3 examples of integral membrane proteins

A

Channels
Transporters
Many receptors

30
Q

What is the function of structural integral membrane proteins?

A

Attaches to intracellular cytoskeleton to hold together cell structure

31
Q

What is the function of enzymes?

A

Integral membrane protein with an active site that is exposed to substrates in the extracellular matrix. Catalyses chemical reactions

32
Q

What is the function of receptor proteins?

A

Integral membrane protein that has a specific binding site exposed to extracellular matrix. Received signals from specific molecules for cellular communication

33
Q

What is the function of marker proteins?

A

Attach to specific non-protein components. Important functions in cellular immunity

34
Q

What is the function of cell adhesion proteins?

A

Allow cells to be held together closely with neighbouring cells. Can allow passage of molecules between cells

35
Q

What is the function of selective ion transport proteins?

A

Integral membrane proteins that allow selective passage of molecules across membranes. These proteins include protein channels for diffusion and osmosis and and carrier proteins involved in active transport

36
Q

Define the term ligand

A

A substance that binds to a protein

37
Q

State the regions of proteins that are involved in ligand binding

A

Free R-groups

38
Q

What are the similarities between the ligand and the protein binding site

A

They have complementary shape and chemistry

39
Q

Name the type of proteins DNA is bound around

A

Histones

40
Q

What is the type of charge on the DNA backbone and the proteins with which it is bound?

A

DNA backbone is negatively charged and the proteins it is bound around are positively charged

41
Q

What structure is formed from DNA and the proteins it is bound to?

A

Nucleosomes

42
Q

What is the name given to the linear structure that results from the tight packaging of DNA in eukaryotes?

A

Chromosomes

43
Q

Name and state the functions of other proteins that bind to specific sequences of double stranded DNA

A

Transcripting factor proteins

Proteins that bind to specific sequences of double stranded DNA and initiate and halt transcription by recruiting DNA polymerase

44
Q

Describe the changes that occur to a protein following the binding of a ligand

A

Results in a conformational change to the protein which therefore alters the behaviour of the protein

45
Q

Name the site where a ligand binds to an enzyme

A

Active site

46
Q

Name the different groups of enzymes? (7)

A 
Protease
ATPase
Phosphatase
Nuclease
Kinase
Synthase
Polymerase
47
Q

What reaction does protease catalyse?

A

Hydrolysis of peptide bonds (breaking down proteins)

48
Q

What reaction does ATPase catalyse?

A

Hydrolysis of ATP

49
Q

What reaction does phosphatase catalyse?

A

Removal of phosphate by hydrolysis

50
Q

What reaction does nuclease catalyse?

A

Breakdown of nucleus acids by hydrolysis

51
Q

What reaction does kinase catalyse?

A

Transfer of a phosphate group to another molecule

52
Q

What reaction does synthase catalyse?

A

The joining of two molecules together by dehydration synthase reaction

53
Q

What reaction does polymerase catalyse?

A

Addition of molecules in series in a chain

54
Q

Describe the induced fit model

A

The active site closely fits the substrate then changes slightly to achieve a perfect fit

55
Q

What happens to the chemical environment when binding of enzyme and substrate occurs

A

The chemical environment produced lowers the activation energy required for the reaction

56
Q

What is the affinity of the enzyme for the
•substrate
•products of a reaction

A

Substrate - high affinity

Products of the reaction - low affinity

57
Q

What happens to the conformation of the enzyme after catalysis?

A

After catalysis the products are released from the active site and the enzyme reverts to its original confirmation

58
Q

Define allosteric enzyme

A

An enzyme that can have its activity altered by a ligand called a modulator

59
Q

Define the term modulator

A

A modulator is is ligand which binds to a secondary binding site separate from the active site (an allosteric site), leading to a conformational change to the enzyme

60
Q

What is the difference between positive and negative modulators of enzyme activity

A

Negative modulators switch off enzymes

Positive modulators switch on enzymes

61
Q

Name the protein structure that can show cooperativity

A

Quaternary protein structure

62
Q

Describe the process of cooperativity

A

When changes in one protein binding site change the affinity of all other sub groups

63
Q

Give an example of a protein that shows cooperativity and state what it does

A

Haemoglobin

Carries oxygen around the body

64
Q

How do pH and temperature affect cooperativity in enzymes

A

High temperature reduces affinity

Low pH reduces affinity

65
Q

What is phosphorylation?

A

The addition or removal of a phosphate group resulting in a reversible confrontational change to the protein which can regulate activity. It’s is a form of post translational modification

66
Q

What is the role of:
•kinase
•phosphatase
•ATPase

A

Kinase transfers a phosphate group (phosphorylation)
Phosphatase removes a phosphate group (dephosphorylation)
ATPase hydrolyses ATP by removing phosphate

67
Q

Describe the adding or removing of a phosphate from a protein

A

Results in a conformational change as the position of charged binding is altered

68
Q

What is the correct term for removing a phosphate from a protein?

A

Dephosphorylation

69
Q

Name 2 types of protein that can be regulated using post translational addition of phosphate

A

Enzymes

Receptors

70
Q

Name the group of proteins that use ATP for their phosphorylation

A

ATPase ?

71
Q

Describe the steps in muscle contraction

A

Muscle contraction occurs when the muscle relieves impulse from a nerve cell
The impulse causes myosin binding sites on actin to be exposed
The myosin heads form a flexed shape and bind to the actin
ADP and Pi are released from myosin, causing it to return to its relaxed shape. This moves the actin filament to the centre of the sarcomere
ATP binds to the myosin head, which causes it to release the actin
The myosin head acts as an ATPase; it breaks down the ATP to ADP and Pi causing the head of the myosin to flex again
(Sarcomere basic unit of muscle)

Advanced Higher Biology (13 decks)

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