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B12 > Proteins (2.5) > Flashcards

Proteins (2.5) Flashcards

1
Q

Describe the function of enzymatic proteins

A

Act as catalysts in cellular reactions

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2
Q

State 2 classifications of enzymatic proteins

A
  1. catabolic enzymes

2. anabolic enzymes

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3
Q

Provide 2 examples of catabolic enzymes

A
  • lipase

- amylase

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4
Q

Provide 1 example of an anabolic enzyme

A
  • DNA polymerase
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5
Q

Describe the function of hormonal proteins

A

Coordinate an organism’s activities by triggering a response

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6
Q

Provide 2 examples of hormonal proteins

A
  • insulin

- glucagon

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7
Q

Describe the 2 major functions of immunological proteins

A
  1. Protect against disease by recognising foreign bodies and microbes
  2. Activate immune cells
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8
Q

Describe the function of contractile proteins

A

Aid muscle contraction

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9
Q

Describe the function of motor proteins

A

Responsible for the movement of cilia and flagella

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10
Q

Provide 2 examples of immunological proteins

A
  • immunoglobulins (antibodies)

- major histocompatibility complex proteins

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11
Q

Provide 2 examples of contractile and motor proteins

A
  • myosin

- actin

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12
Q

Describe the function of structural proteins

A

Provide support by forming cellular structures and assist in contractile tissue function

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13
Q

Provide 2 examples of structural proteins

A
  • collagen

- cytoskeleton

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14
Q

Describe the function of transport proteins

A

Transport of substances through carrier and channel proteins across a semipermeable membrane

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15
Q

Provide 2 examples of transport proteins

A
  • haemoglobin
  • sodium-potassium pump
  • calcium channel
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16
Q

Describe the function of receptor proteins

A

Assist the cell in responding to a chemical stimuli

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17
Q

Provide 2 examples of receptor proteins

A
  • neurotransmitter receptors

- hormone receptors

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18
Q

Describe the function of storage proteins

A

Storage of metal ions and amino acids

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19
Q

Provide 2 examples of storage proteins

A
  • casein (stores amino acids)

- ferritin (stores iron)

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20
Q

Describe proteome

A

Complete set of proteins expressed by the genome

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21
Q

Describe the genome

A

Complete set of genes or genetic material of an individual cell or organism.

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22
Q

State what the proteome varies between

A
  • cell type
  • developmental stage
  • environmental conditions
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23
Q

State the factor that controls the production of proteins within cells

A

Expression or ‘switching on’ of specific genes in a genome

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24
Q

Describe proteomics

A

Study of the structure, function, interactions of proteins

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25
Q

State the composition of all proteins

A

Amino acids

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26
Q

State the 3 structures that compose the structure of amino acids

A
  1. Amine group
  2. Carboxyl group
  3. Variable R group
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27
Q

State the chemical composition of the amine group of amino acids

A

NH2

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28
Q

State the chemical composition of the carboxyl group of amino acids

A

COOH

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29
Q

State how many standard amino acids are involved in the synthesis of proteins within organisms

A

20 amino acids

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30
Q

Provide 3 examples of the variable characteristics of the amino acid ‘R group’

A
  1. Charged/uncharged
  2. Polar/non-polar
  3. Hydrophobic/hydrophilic
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31
Q

Define condensation polymerisation

A

The reaction in which monomers are joined to create a polymer by the removal of water

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32
Q

Explain the process of condensation polymerisation in the synthesis of dipeptides

A

Hydrogen/oxygen (carboxyl group) + hydrogen (amine group) -> water
Dipeptide is synthesised with a peptide bond holding the two amino acids together

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33
Q

Describe polypeptide chain

A

Chain of amino acids joined by peptide bonds

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34
Q

Describe what forms the backbone of the polypeptide chain

A

Repeats of the carboxyl and amine groups

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35
Q

Describe what forms the side chains of the polypeptide chains

A

R groups

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36
Q

Define proteins

A

Organic compound consisting of one or more long chains of amino acids, connected by peptide bonds

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37
Q

State what most proteins are required to do…

A

Bind to other molecules

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38
Q

Describe the impact of a single change to one amino acid within a sequence

A

Can alter the shape and overall function of a protein

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39
Q

State the 4 different levels of organisation when describing the structure of a protein

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quaternary
40
Q

Describe primary structure

A

Linear sequence of amino acids in the polypeptide chain

41
Q

Describe the significance of the linear sequence

A

The linear sequence:

  • provides information on how proteins will fold
  • compares functional and non-functional proteins (identify what changes to the sequence render protein non-functional)
  • provide evolutionary history of the protein
42
Q

State whether the linear sequence of a protein is unique to every protein. True/false.

A

True

43
Q

State the first level of protein organisation

A

Primary structure

44
Q

State the second level of protein organisation

A

Secondary structure

45
Q

State the third level of protein organisation

A

Tertiary structure

46
Q

State the fourth level of protein structure

A

Quaternary structure

47
Q

Explain what causes the folding of the polypeptide chain in the secondary level of organisation

A

Hydrogen bond formation between the amine and carboxyl groups of amino acids

48
Q

State the 3 major types of secondary structures

A
  1. Alpha helix
  2. Beta-pleated sheets
  3. Random coil
49
Q

Describe the process surrounding the formation of the alpha helix structure of secondary proteins

A

Formation of hydrogen bonds between adjacent amine and carboxyl groups within the polypeptide chain (causes the chain to coil into a helical shape)

50
Q

Describe the process surrounding the formation of the beta-pleated sheet structure of secondary proteins

A

Hydrogen bonds form between amine and carboxyl groups in different parts of the adjacent polypeptide chains, causing the chains to fold back on each other

51
Q

Describe the random coil structure of secondary proteins

A

Parts of the polypeptide chain appear to have a random structure, however the same pattern of folding occur in all molecules of the same protein.
(E.g. all insulin molecules will have the same random coil structure)

52
Q

Describe the formation of a functional protein in the tertiary level of organisation

A

Further folding of polypeptides, forming more stable globular or fibrous 3D shapes

53
Q

State what tertiary protein structure is usually a combination of…

A

Alpha helices and beta-pleated sheets

54
Q

State the unique types of bonds associated with tertiary protein structure

A
  • disulfide bridge formation
  • hydrogen bonds
  • hydrophobic packing
  • van der Waal interactions
55
Q

State whether the tertiary structure is the final structure for some proteins. True/false.

A

True

56
Q

Outline the factor encouraging the spontaneous folding of smaller tertiary-structured polypeptides

A

Chemical environment

57
Q

Outline the factor required by large, complex proteins in assisting them to fold correctly and refold if they denature

A

Specialised proteins (chaperonins)

58
Q

Define denature

A

Irreversible change in tertiary protein structure that results in the loss of function.

59
Q

Describe the formation of a functional protein in the quaternary level of organisation

A

Two or more polypeptide chains join together (polypeptides may be identical or different)

60
Q

State what a protein with a prosthetic group is known as

A

Conjugated protein

61
Q

Describe prosthetic groups

A

Inorganic compound that is involved in protein structure or function

62
Q

Describe conjugated protein

A

Protein that contains a non-protein group

63
Q

Provide 1 example of a conjugated protein

A

Haemoglobin

64
Q

Describe chaperonins

A

Protein molecules that assist in the proper folding of other proteins

65
Q

State what chaperonins provide polypeptides with

A

Area to fold in without the influence from the cytoplasmic environment, such as changes in pH

66
Q

State the 2 types of protein classification

A
  1. Fibrous proteins

2. Globular proteins

67
Q

Describe fibrous proteins

A

Elongated and insoluble (structural roles)

68
Q

Provide 2 examples of fibrous proteins

A
  • collagen (connective tissue)

- keratin (hair and nails)

69
Q

Describe globular proteins

A

Compactly folded and coiled (spherically shaped) and generally soluble

70
Q

Outline the structure of globular proteins (e.g. core and outer region)

A

Hydrophobic core

Hydrophilic outer region

71
Q

Provide 2 examples of globular proteins

A
  • enzymes

- hormones

72
Q

Provide a major factor supporting the loss of function of a protein

A

Denaturation

73
Q

State 3 factors of the environment that affect protein structure and function

A
  • temperature
  • pH
  • concentration of ions/molecules that act as cofactors
74
Q

Describe the structural changes of a protein due to denaturation

A
  • hydrogen bonds
  • disulfide bridges
  • hydrophobic interactions
  • van der Waals forces
    … broken - altering protein shape
75
Q

State what a protein which is partially denatured may be able to do…

A

Fold again (renature)

76
Q

Describe the effect of temperature on protein function

A
  • high temp -> denaturation due to bond breakage

- low temp -> bonds are not flexible enough to accommodate conformational changes

77
Q

Describe the effect of pH on protein function

A

Protein tertiary structure is affected when the pH leaves optimal range

78
Q

Describe the effect of cofactors on protein function

A

Some proteins require non-protein chemical compounds for their biological function.

79
Q

Provide 1 example of a cofactor and its’ effect on protein function

A

Magnesium - cofactor
Essential for chlorophyll function
Lack of magnesium results in yellowing of leaves

80
Q

Describe anabolic reaction

A

Biochemical reaction in which larger molecules are made from smaller molecules, which requires an input of energy to build new bonds.

81
Q

Describe catabolic reaction

A

Biochemical reaction in which there is a breakdown of macromolecules into smaller molecules, releases energy.

82
Q

State the 2 major classes of beta pleated sheets

A
  1. antiparallel beta sheets

2. parallel beta sheets

83
Q

Describe parallel beta sheets

A

Two peptide strands running in the same direction held together by hydrogen bonds

84
Q

Describe the antiparallel beta sheet

A

Two peptide strands run in opposite direction held together by hydrogen bonds

85
Q

Describe the alpha carbon

A

Carbon atom next to the carboxyl group

86
Q

Describe cleaving as a protein modification

A

Cleaving of polypeptide chains to give smaller chains, that may fold or join to produce functional proteins

87
Q

Describe glycosylation as a protein modification

A

Addition of a carbohydrate tag to assist in cell recognition

88
Q

Describe phosphorylation as a protein modification

A

Addition of phosphate groups to contribute to proteins 3D shape or assist in signalling

89
Q

Describe lipid attachment as a protein modification

A

Lipids attached to them which anchor the protein to the plasma membrane

90
Q

Describe degradation

A

Polypeptide chains tagged for degredation when they are no longer useful - amino acids are reused in the formation of other proteins

91
Q

Describe level of folding of globular proteins

A

Tertiary or quaternary folding

92
Q

Describe level of folding of fibrous proteins

A

Little or no tertiary folding

93
Q

Where is DNA located in cells?

A

Nucleus

94
Q

State what the functional diversity of proteins is explained by

A

Amino acids being assembled into a variety of polypeptide chains

95
Q

Describe polymerise

A

Production of a large molecule from many repeating smaller units by CPR

96
Q

Describe the process by which an amino acid chain is synthesised

A

Peptide bond forms by CPR between the COOH end of one amino acid and the amino end of another amino acid

97
Q

State what can different proteins to be produced when expressing the same gene

A

Removal of different arrangements of introns

B12 (41 decks)

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