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Protiens Flashcards

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Biology 101 flashcards
1
Q

What elements do proteins contain ?

A

C, H, O, N, (sometimes) S

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2
Q

What are the monomers that make up proteins ?

A

Amino acids

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3
Q

What is the structure of an AA?

A

Consists of 1 central C atom bonded to a H atom, a Carboxylic group (-COOH), and amino group (-NH2) and a specific side chain/ R-group

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4
Q

What do R-groups determine ?

A

Property of AA

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5
Q

What are the four types of AA

A

Neutral and non-polar
Neutral and polar
Acidic and polar
Basic and polar

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6
Q

Which R groups are hydrophilic and which are hydrophobic ?

A

Polar forms H bond with water - hydrophilic
Non-polar cannot form H bonds - hydrophobic

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7
Q

How to categories the R groups into the four categories

A

Neutral and non-polar : no charge, no S,O,N
Neutral and polar : no charge, contains S O N
Acidic and polar : negative charge
Basic and polar : positive charge

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8
Q

What are the properties of AA?

A

Colourless
Crystalline solids
Generally soluble in water but insoluble in inorganic solvents
Dissolves in water to form ions : -NH2 to -NH3+ and -COOH to -COO-
Amphoteric : exhibits both acid and basic properties
Zwitterions formed when both amino and carboxyl group fully ionised

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9
Q

What are zwitterions ?

A

Molecules that bear charged groups of opposite polarities

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10
Q

What is the isoelectricc point ?

A

pH at which AA exists mainly in its zwitteroin form

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11
Q

What is electrophoresis ?

A

Separation technique based on the movement of charged ions under the influence of an electrical field

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12
Q

What type of AA move towards which end in electrophoresis ?

A

AA with net positive charge move towards the negative electrode (cathode)
AA with net negative charge move towards the positive electrode (anode)

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13
Q

What bond is formed between AAs?

A

Peptide bond (-CONH-)

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14
Q

What is the direction of a polypeptide ?

A

1st AA : amino end ( N terminus)
Last AA : carboxyl end ( C terminus)

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15
Q

What are the four levels of organisation ?

A

Primary structure
Secondary structure
Tertiary structure
Quaternary structure

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16
Q

What does primary structure refer to ?

A

Type, number and sequence of AAs linked by peptide bonds

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17
Q

Why is primary structure important ?

A

Determines properties and 3D shape of polypeptide
Determine biological function of polypeptide

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18
Q

What does secondary structure refer to ?

A

Localised folds and coils that occur in the polypeptide chain

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19
Q

How are the folds and coils in secondary structure formed ?

A

Formed as a result of interchain H bond at reglar intervals along polypeptide backbone between AA lying close to each other

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20
Q

Is R group interaction involved in secondary structures ?

A

No

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21
Q

What are the two types of secondary structures ?

A

Alpha-helix (a-helix)
Beta-pleated sheet (ß-pleated sheet)

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22
Q

How is a-helix formed ?

A

The oxygen of the carbonyl group of residue n forms H bond with the H of the amino group of residue (n+4)

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23
Q

What is the structure of a-helix ?

A

The helix backbone winds around long axis resulting in right-hand coil with H bonds all aligned parallel to axis while the R groups project outward
Inter-chain H bonds stabilise the a-helix

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24
Q

How many AA (avg) are there per complete turn in the a-helix ?

A

3.6

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25
Q

What is a ß-pleated sheet ?

A

A structure comprising of 2 or more adjacent regions (ß strands) of a polypeptide chain held by multiple intracranial H bonds at regular intervals

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26
Q

What are the two types of ß-pleated sheets?

A

Parallel ß-pleated sheets : adjacent ß-strand run in same direction
Anti-parallel ß-pleated sheet : adjacent ß strand run in opposite direction

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27
Q

Where are the R groups projected in ß-pleated sheet?

A

Above and below the ß-pleated sheet

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28
Q

Usually which type of R groups (hydrophilic or hydrophobic) on AA makes up the ß strand ?

A

The composition of ß strands tend to favour AA with hydrophobic R-groups

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29
Q

What is tertiary structure ?

A

When polypeptide folds extensively upon itself to form a precise compact globular shape involving R group interactions between AA that are far away from one another

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30
Q

what are the types of R group interactions between AA in tertiary structure ?

A

Disulfide bond (covalent)
H bond
Ionic interaction
Hydrophobic interaction

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31
Q

Why is tertiary structure important ?

A

It allows important AA residues that are far away to be brought together into localised region
- these regions often act as proteins active site, binding site and functional site

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32
Q

What does tertiary structure look like ?

A

Globular shape of protein with distinct / 3D conformation

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33
Q

Are tertiary structures soluble in water ?

A

Yes

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34
Q

Why are tertiary structures soluble in water ?

A

Hydrophobic R groups are hidden in the interior of the protein molecule while the hydrophilic R groups are exposed to the aqueous external environment

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35
Q

Can proteins with tertiary structure also have secondary structure present ?

A

Yes

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36
Q

What is quaternary structure ?

A

Association of two or more polypeptide chains held together by hydrophobic interactions, H bonds and ionic interaction to form a precise structure

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37
Q

What are ionic bonds ?

A

Electrostatic attraction between oppositely changes R groups from different parts of the chain

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38
Q

Is formation of ionic bond dependent on pH ?

A

Very dependent
- ionisation of the R groups depend on the pH the AA is exposed to

39
Q

Are ionic bonds weak or strong ?

A

Relatively weak (non-covalent)
- easily interrupted by change in pH and temperature
- ionisation of R groups depend on pH

40
Q

When are H bonds formed ?

A

Formed when a H atom that is covalente bonded to an electronegative atom ( usually N, O) is simultaneously attracted to another electronegative atom

41
Q

What are hydrophobic interactions ?

A

When non-polar (hydrophobic) R groups cluster together in water forming weak associations called hydrophobic interactions

42
Q

What are disulfide linkages ?

A

Bond formed between two sulfur atoms on different R groups (cysteine residues - contain sulfur)

43
Q

How is the 3D structure of a protein disrupted ?

A

Change in temperature
Change in pH
Concentration of salts and reducing agents

44
Q

What is denaturation ?

A

Change to the specific 3D shape of polypeptide chains due to unfolding of chains, resulting in loss of function / biological activity

45
Q

Does desaturation affect primary structure ?

A

No since it does not involve hydrolysis of peptide bonds

46
Q

Which structure(s) does denaturation involve ?

A

Secondary
Tertiary
Quaternary

47
Q

How does temperature affect protein ?

A

Heat can be used to disrupt H bonds, ionic bonds and non-polar hydrophobic interactions
Heat increases the kinetic energy of and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted

48
Q

How does pH affect the protein ?

A

Acids and bases disrupt ion in bonds between AA of a polypeptide

Additional H+ ions in acids combine with teh -COO- group on AA and form -COOH
Reduced number of H+ ions cause NH3+ groups to lose H+ ions and form NH2

49
Q

How does metal salts and reducing agents affect protein ?

A

Heavy metal salts denature proteins in similar way as pH since these salts are charged

Reducing agents may disrupt disulfide bonds which are formed through oxidation

50
Q

What is an example of a transport protein ?

A

Haemoglobin

51
Q

What is haemoglobin ?

A

It is found in RBCs as an oxygen-carrying globular protein associated with a non-protein heme group which contains Fe2+

52
Q

How many polypeptide chains are haemoglobin made of ?

A

4 - 2 are (a chains) and 2 are (ß chains)

53
Q

What kind of secondary structure exists in haemoglobin ?

A

Only a-helixes

54
Q

What is the primary structure in haemoglobin ?

A

Interactions between AA that are far away result in extensive folding and coiling of the polypeptide chain
- gives rise to specific 3D conformation where a hydrophobic cleft lined with hydrophobic AA is formed
- provides hydrophobic environment for heme group that is largely hydrophobic

55
Q

How is haemoglobin a good transport protein - structure and function (tertiary structure) ?

A

Compact and globular : allows more to be packed into a RBC for transport of oxygen

The four polypeptide chains coils closely together, there hydrophobic side chains are pointing towards the center while the hydrophilic groups point outwards : making haemoglobin soluble in aqueous mediums thus a good transport protein

56
Q

What is cooperative binding in haemoglobin ?

A

Where the binding of oxygen to one heme group facilitates the binding of oxygen to the other heme groups on the same molecule

57
Q

What is a heme group made up of?

A

Porphyria rings and iron ion (Fe2+)

58
Q

What is the structure of a heme group ?

A

The Fe2+ is at the centre of the porphyrin ring and the heme is orientated such that the Fe2+ on one face is complexed to an AA residue leading the other face for binding oxygen

59
Q

How many heme groups are there in one haemoglobin ?

A

4
- 1 bonded to each polypeptide

60
Q

What is the maximum number of oxygen that a haemoglobin can carry at one time ?

A

4 - 1 per each heme group

61
Q

How is heme held in place in the haemoglobin ?

A

By weak bonds between heme and some of the R groups in the polypeptide

62
Q

Are haemoglobin pH and temperature dependent ?

A

Yes

Presence of non-covalent bonds (ionic bond, hydrophobic interactions, H bonds) important in holding the enzyme in shape, thus sensitive to pH and temperature

63
Q

What type of mutation occurs to result in sickle cell anemia ?

A

Gene mutation which leads to a change in primary structure

64
Q

Which structure in haemoglobin is affected in sickle cell anemia ?

A

Primary structure

65
Q

What is mutated in sickle cell anemia ?

A

Gene mutation in the R group chain of the haemoglobin causes a change of one AA : valine is coded for instead of glutamic acid

66
Q

What is the mutated haemoglobin called ?

A

Haemoglobin S (HbS)

67
Q

What is the difference between valine and glutamic acid that causes sickle cell anemia ?

A

Valine is hydrophobic while glutamic acid is hydrophilic : solubility of the deoxygenated HbS decreases

68
Q

How does the change in primary structure due to mutation affect haemoglobin’s function ?

A

HbS molecules will aggregate (lock together) and become rigid, precipitating out of solution, causing RBC to collapse

HbS will chain together forming stiff rod-like structures within the el which changes the RBS into a sickle shape : sickle-shaped cells are not flexible and can stick to vessel walls, causing blockage that slows or stops the flow of blood thus oxygen is not able to reach nearby tissues

69
Q

What is collagen ?

A

Main protein found in connectivity tissue in animals

Responsible for skin strength and elasticity together with soft keratin

70
Q

Why is collagen important ?

A

It is an important structural protein essential to creating the body’s physical structure as an extracellular matrix acting as a supporting framework over which cells are arranged

71
Q

Describe the primary structure of collagen

A
  • rich in AA glycine and propine, every third AA is glycine which is the smallest AA
  • contains modified AA hydroxyproline and hydroxylysine
  • has a repeating sequence of gly-x-y where x is usually proline and y is often hydroxyproline
72
Q

What makes up one tropocollagen ?

A

3 polypeptide chains (~1000 AA) wound tightly around each other to form a triple helix

73
Q

Describe the secondary structure of collagen

A

Kinked helix formed by polypeptide chain where there is a sharp change in the direction of the helix axis
- kinks allow the 3 helix to wound around each other more tightly to form tropocollagen
- glycine fits nicely into the interior of the triple helix

74
Q

As a whole, which level of structure does tropocollagen show ?

A

Quaternary

75
Q

How is each tropocollagen stable ?

A

Interchain H bonds formed between the three polypeptide chains
- between the -NH group of glycine and the -CO group of residues on neighbouring chains

76
Q

What is a collagen fibril ?

A

Where each complete tropocollagen interacts with other tropocollagen running parallel to it, forming covalent bonds between side chains (R groups) of the lysine residues which hold many tropocollagen molecules side by side

77
Q

How are the tropocollagen arranged in a collagen fibril ? Why ?

A

Parallel chains of tropocollagen molecules are in staggered arrangement
- eliminated presence of weak area
- results in banded appearance of fibrils

78
Q

What are collagen fibres ?

A

Collagen fibrils further aggregate into collagen fibres

79
Q

Where does the assembly of collagen fibres occur ?

A

Outside the cell

80
Q

What is the most important level of organisation in collagen ?

A

Secondary structure

81
Q

How does the secondary structure of collagen relate to its function as a structural protein ?

A

Collagen is fibrous or strand-like
- allows for larger surface area for cross-linking (H bonds) so as to increase tensile strength

82
Q

How does the primary structure of collagen relate to its function ?

A

AA sequence and length is not very specific
- depending on the AA sequence present, different types of collagen can result

83
Q

Is collagen soluble in water ?

A

Insoluble due to large molecular size consisting of many hydrophobic AA ( glycine, proline)

Thus making it highly stable and fit for being a structural protein

84
Q

Where does collagen exhibit high tensile strength ?

A

Within each subunit
Between tropocollagen
Aggregation into collagen fibrils

85
Q

How does tropocollagen contribute to collagen tensile strength ?

A

Within each tropocollagen
-3 polypeptides tightly coiled together mean that more force is required to break the tropocollagen compared to it being made up of only one polypeptide
- strand-like structure of each polypeptide means greater surface area exposed for more cross-linking (interchain H bond) which will stabilise the structure

Between tropocollagen
- staggered arrangement of tropocollagen ensures that there are no weak areas
- covalent cross-links formed between tropocollagen further strengths the structure

86
Q

What is a G-protein coupled receptor ?

A

The largest group of plasma membrane receptors (embedded in the membrane, sere to receive signals)
- integral palms membrane proteins that transduce signals from extracellular ligands to signals in intracellular relay proteins (G proteins)

87
Q

What are G proteins ?

A

Function as molecular switch (inside cell) that are either on or off

88
Q

When are G proteins active ?

A

When GTP (guanosine triphosphate) bound

89
Q

When are G proteins inactive ?

A

When GDP (guanosine diphosphate) bound

90
Q

What is the structure of G protein coupled receptor ?

A

Structural signature of 7 hydrophobic transmembrane a-helix segments with extracellular N terminus and intracellular C terminus

91
Q

What is the secondary structure of the G-protein coupled receptor ?

A

Each of the transmembrane regionals contain an a-helix where r hydrophobic AA face outwards to the hydrophobic core of the plasma membrane

92
Q

How does the secondary structure of the g-protein coupled receptor relate to its function as signalling protein ?

A

Allows for the receptor to be embedded within the plasma membrane

93
Q

How are the specific binding sites on the G-protein coupled receptor formed ?

A

Specific loops between the helixes form specific 3D conformation for extracellular binding sites for signalling molecules and intracellular binding sites for G protein molecules

94
Q

How does the specific binding sites on the g-protein receptor relate to its function as signalling protein ?

A

Allows for specific signalling ligands to bind to the receptor and activate receptor to interact with specific G proteins

bio (23 decks)

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