Topic 7.5: Proteins Flashcards

(50 cards)

1
Q

Explain Primary (1°) Structure of Protein (3)

A

The order / sequence of the amino acids of which the protein is composed
Formed by covalent peptide bonds between adjacent amino acids
Controls all subsequent levels of structure because it determines the nature of the interactions between R groups of different amino acids

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2
Q

Explain Secondary (2°) Structure of Protein (4)

A

The way the chains of amino acids fold or turn upon themselves
Held together by hydrogen bonds between non-adjacent amine (N-H) and carboxylic (C-O) groups
May form an alpha helix, a beta-pleated sheet or a random coil
Secondary structure provides a level of structural stability (due to H-bond formation)

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3
Q

Explain Tertiary (3°) Structure of Protein (3)

A

The way a polypeptide folds and coils to form a complex molecular shape (e.g. 3D shape)
Caused by interactions between R groups; including H-bonds, disulphide bridges, ionic bonds and hydrophilic / hydrophobic interactions
Tertiary structure may be important for the function of the enzyme (e.g. specificity of active site in enzymes)

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4
Q

Explain Quaternary (4°) Structure of Protein (4)

A

The interaction between multiple polypeptides or prosthetic groups that results in a single, larger, biologically active protein
A prosthetic group is an inorganic compound involved in protein structure or function (e.g. the heme group in haemoglobin)
A protein containing a prosthetic group is called a conjugated protein
Quaternary structure may be held together by a variety of bonds (similar to tertiary structure)

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5
Q

What is the difference between a fibrous protein and globular protein in respect to shape?

A

Fibrous: long and narrow

Globular: round/spherical

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6
Q

What is the difference between a fibrous protein and globular protein in respect to role?

A

Fibrous: structural (strength and support)

Globular: functional (catalytic, transport, etc)

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7
Q

What is the difference between a fibrous protein and globular protein in respect to solubility?

A

Fibrous: (generally) insoluble in water

Globular: (generally) soluble in water

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8
Q

What is the difference between a fibrous protein and globular protein in respect to sequence?

A

Fibrous: repetitive amino acid sequence

Globular: irregular amino acid sequence

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9
Q

What is the difference between a fibrous protein and globular protein in respect to stability?

A

Fibrous: less sensitive to changes in heat, pH, etc

Globular: more sensitive to changes in heat, pH, etc

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10
Q

What is the difference between a fibrous protein (6) and globular protein (4) in respect to examples?

A

Fibrous: collagen, myosin, fibrin, actin, keratin, and elastin

Globular: catalase, hemoglobin, insulin, immunoglobin

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11
Q

Is collagen a fibrous or globular protein?

A

fibrous

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12
Q

Is myosin a fibrous or globular protein?

A

fibrous

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13
Q

Is fibrin a fibrous or globular protein?

A

fibrous

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14
Q

Is actin a fibrous or globular protein?

A

fibrous

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15
Q

Is keratin a fibrous or globular protein?

A

fibrous

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16
Q

Is elastin a fibrous or globular protein?

A

fibrous

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17
Q

Is catalase a fibrous or globular protein?

A

globular

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18
Q

Is hemoglobin a fibrous or globular protein?

A

globular

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19
Q

Is insulin a fibrous or globular protein?

A

globular

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20
Q

Is immunoglobin a fibrous or globular protein?

A

globular

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21
Q

Explain the significance of polar and non-polar amino acids (4)

A

Polar amino acids have hydrophilic R groups, whereas non-polar amino acids have hydrophobic R groups
For water soluble proteins, non-polar amino acids tend to be found in the centre of the protein (stabilising structure) while polar amino acids are found on the surface (capable of interacting with water molecules)
For membrane-bound proteins, non-polar amino acids tend to be localised on the surface in contact with the membrane, while polar amino acids line interior pores (to create hydrophilic channels)
For enzymes, the active site specifically depends on the location and distribution of polar and non-polar amino acids as hydrophobic and hydrophilic interactions can play a role in substrate binding to the active site

22
Q

What are the six functions of proteins?

A

structure, hormones, immunity, transport, movement, and enzymes

23
Q

What is the role of structure proteins?

A

Support for body tissue

24
Q

What is the role of hormone proteins?

A

Regulation of blood glucose

25
What is the role of immunity proteins?
Bind antigens
26
What is the role of transport proteins?
Oxygen transport
27
What is the role of movement proteins?
Muscle contraction
28
What is the role of enzyme proteins?
Speeding up metabolic reactions
29
Name three examples of structure proteins
collagen, elastin, keratin
30
Name two examples of hormone proteins
insulin, glucagon
31
Name two examples of immunity proteins
antibodies / immunoglobulins
32
Name two examples of transport proteins
haemoglobin, myoglobin
33
Name four examples of movement proteins
actin / myosin, troponin / tropomyosin
34
Name three examples of enzyme proteins
catalase, lipase, pepsin
35
What type of protein function does collagen serve?
structure
36
What type of protein function does elastin serve?
structure
37
What type of protein function does keratin serve?
structure
38
What type of protein function does insulin serve?
hormones
39
What type of protein function does glucagon serve?
hormones
40
What type of protein function does antibodies serve?
immunity
41
What type of protein function does immunoglobulins serve?
immunity
42
What type of protein function does hemaglobin serve?
transport
43
What type of protein function does myoglobin serve?
transport
44
What type of protein function does actin serve?
movement
45
What type of protein function does myosin serve?
movement
46
What type of protein function does troponin serve?
movement
47
What type of protein function does tropomyosin serve?
movement
48
What type of protein function does catalase serve?
enzymes
49
What type of protein function does lipase serve?
enzymes
50
What type of protein function does pepsin serve?
enzymes