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IB Biology > 2.4 Proteins > Flashcards

2.4 Proteins Flashcards

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1
Q

What are proteins comprised of?

A

Long chains of amino acids

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2
Q

What do all amino acids share?

A

A common basic structure

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3
Q

What is the basic structure of amino acids?

A

A central carbon atom attached to an amine group, a carboxylic acid group, a hydrogen atom and a variable side chain

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4
Q

How many different amino acids are there?

A

20

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4
Q

Where are amino acids joined together?

A

On the ribosome

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5
Q

What are the long chains of amino acids called?

A

Polypeptides

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6
Q

What do polypeptides make up?

A

Proteins

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7
Q

How does each type of amino acid differ?

A

The composition of the variable side chain

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8
Q

What causes each proteins fold and function differently?

A

Because they have a different distinct chemical properties

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9
Q

Why do proteins fold and function differently?

A

To work in accordance to its specific position within the polypeptide chain

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10
Q

Why are organisms capable of producing a huge range of possible polypeptides?

A

Because most polypeptide chains have 50 - 2000 amino acid residues

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11
Q

What is the bonding between amino acids?

A

Covalent bonding

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12
Q

What type of reaction is needed to join amino acids?

A

Condensation reaction

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13
Q

What is the covalent bond between the amino acids called?

A

A peptide bond

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14
Q

How can polypeptide chains be broken down?

A

Hydrolysis reactions

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14
Q

What does amino acids joining together form?

A

A dipeptide and water

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15
Q

What does the breakdown of polypeptide chains require and why?

A

Water to reverse the process

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16
Q

Where do the peptide bonds form?

A

Between the amine and carboxylic acid groups of adjacent amino acids

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17
Q

What forms water during the formation of a peptide bond?

A

The amine group losing a hydrogen atom and the carboxylic acid loses a hydroxyl (OH) creating water

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18
Q

What is the order of amino acid sequence called?

A

Primary structure

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19
Q

What does primary structure determine?

A

The way the chain will fold

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20
Q

Why will different amino acid sequences fold into different configurations?

A

Due to the chemical properties of the variable side chains

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21
Q

What will amino acids commonly fold into?

A

Secondary structures

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22
Q

What is it called when the amino acids fold into two stable configurations?

A

Secondary structures

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23
Q

When do alpha helices occur?

A

When the amino acid sequence folds into a coil/spiral arrangement

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24
Q

When do beta pleated sheets occur?

A

When the amino acid sequence adopts a directionally oriented staggered strand conformation

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25
Q

What causes both alpha helices and beta pleated sheets?

A

Hydrogen bonds forming between non adjacent amine and carboxyl groups

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26
Q

What happens when no secondary structure exists?

A

The polypeptide chain will form a random coil

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27
Q

What is the tertiary structure?

A

The overall three dimensional configuration of the protein

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28
Q

What determines the tertiary structure of a polypeptide chain?

A

The interactions between the variable side chains

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29
Q

What are four examples of interactions between the variable side chains?

A

Hydrogen bonds
Disulphide bridges
Ionic interactions
Polar associations

30
Q

What affects the overall shape of the polypeptide chain?

A

The affinity or repulsion of side chains

31
Q

What determines all levels of protein folding?

A

Primary structure

32
Q

What determines the affinity or repulsion of side chains?

A

The position of specific amino acids within a sequence

33
Q

What is it called when certain proteins have a fourth level of structural organisation?

A

Quarternary structure

34
Q

Where do you find quaternary structures?

A

In proteins that have more than one polypeptide chain linked together

35
Q

What type of structure is it when a protein has an inorganic prosthetic group as part of their structure?

A

Quaternary structure

36
Q

Will all proteins have a quaternary structure and explain your answer?

A

No as many proteins only have a single polypeptide chain

37
Q

What is an example of a protein with a quaternary structure?

A

Haemoglobin

38
Q

How many and what polypeptide chains does haemoglobin have?

A

Four
two alpha chains
Two beta chains

39
Q

Apart from multiple polypeptide chains what does haemoglobin have to make it have a quaternary structure?

A

A prosthetic group

40
Q

What is denaturation?

A

Denaturation is a structural change in a protein that results in the loss of its biological properties

41
Q

What will cause the tertiary structure to alter its activity and why?

A

Any change or abrogation to the tertiary structure as the way a protein folds determines its function

42
Q

What are the two key conditions that can cause denaturation?

A

Temperature and pH

43
Q

What will high levels of thermal energy do to the proteins?

A

Break the hydrogen bonds that holds the protein together, causing them to unfold and lose its ability to function

44
Q

What does changing the pH of a protein do?

A

Alter the charge which alter the proteins solubility and overall shape

45
Q

What is the perfect temperature or pH called?

A

The optimum

46
Q

What is a gene?

A

A gene is a sequence of DNA which encodes a polypeptide sequence

47
Q

What is a gene sequence converted into?

A

A polypeptide sequence

48
Q

What are the two processes that convert gene sequence into a polypeptide sequence?

A

Transcription and translation

49
Q

What does transcription do?

A

Makes an mRNA transcription based on a DNA template

50
Q

What does translation do?

A

Uses the instructions of the mRNA transcript to link amino acids together

51
Q

Typically one gene will code for what?

A

One polypeptide

52
Q

What are the three exceptions to the fact that one gene will code for one polypeptide?

A

Genes may be alternatively spliced to generate multiple polypeptide variants

Genes encoding tRNA sequences are transcribed but never translated

Genes may be mutated and consequently produce an alternative polypeptide sequence

53
Q

What is the proteome?

A

All of the proteins expressed within a cell, tissue or organism at a certain time

54
Q

Why are proteomes of any given individual unique?

A

As protein expression patterns are determined by an individuals gene

55
Q

Is the proteome larger or smaller than the number of genes in an individual?

A

Larger

56
Q

What are the two reasons a proteome may be larger than the genes in a person?

A

Gene sequences may be alternatively spliced following transcription to generate multiple protein variants from a single gene

Proteins may be modified following translation to promote more variations

57
Q

What are the different functions of proteins? (shits me)

A

Structure
Hormones
Immunity
Transport
Sensation
Movement
Enzymes

58
Q

What are two examples of the protein function structure?

A

Collagen
Spider silk

59
Q

What is collagen?

A

Component of the connective tissue of animals

60
Q

What is spider silk?

A

A fibre spun by spiders to make webs

61
Q

What are two examples of the protein function hormones?

A

Insulin
Glucagon

62
Q

What is insulin?

A

Protein produced by the pancreas and triggers a reduction in blood glucose levels

63
Q

What is glucagon?

A

Protein produced by the pancreas that triggers an increase in blood glucose levels

64
Q

What is an example of the protein function of immunity?

A

Immunoglobulins

65
Q

What are immunoglobulins?

A

Antibodies produced by plasma cells that are capable of targeting specific antigens

66
Q

What are two examples of the protein function transport?

A

Haemoglobin
Cytochrome

67
Q

What is haemoglobin?

A

A protein found in red blood cells that is responsible for the transport of oxygen

68
Q

What is cytochrome?

A

A group of proteins located in the mitochondria and involved in the electron transport chain

69
Q

What is an example of the protein function sensation?

A

Rhosopsin

70
Q

What is rhodopsin?

A

A pigment in the photoreceptor cells of the retina that is responsible for the detection of light

71
Q

What are two examples of the protein function movement?

A

Actin
Myosin

72
Q

What is actin?

A

Thin filaments involved in the contraction of muscle fibres

73
Q

What is myosin?

A

Thick filaments involved in the contraction of muscle fibres

74
Q

What is an example of the protein function enzymes?

A

Rubisco

75
Q

What is rubisco?

A

An enzyme involved in the light independent stage of photosynthesis

IB Biology (57 decks)

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