Proteins and Enzymes Flashcards

1
Q

What are the 4 basic categories of amino acids?

A

Acidic
Basic
Polar
Non-polar

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2
Q

What is the primary protein structure a source of?

A

Versatiliy in protein structure and function

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3
Q

What is an enzyme co-factor?

A

A non-protein component needed for activity

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4
Q

In which three main ways do enzymes catalyse reactions?

A

Increase rates of spontaneous reactions
Lower activation energy of biochemical reactions
Accelerate movement towards reaction equilibria

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5
Q

A large Km signifies what?

A

A low affinity of the substrate for the enzyme

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6
Q

What type of protein is an enzyme?

A

Globular protein

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7
Q

Where are co-enzymes usually produced from?

A

A vitamin

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8
Q

Spontaneous reactions must have what type of delta G value?

A

A negative one

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9
Q

Enzymes reduce what in a reaction?

A

The activation energy required

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10
Q

What are the 3 ways that enzymes can reduce activation energy?

A

Entropy reduction
Desolvation
Induced fit

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11
Q

What does a large Vmax indicate?

A

Very fast enzyme

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12
Q

What type of Vmax does glucokinase have?

A

A high Vmax

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13
Q

How can you separate gluco and hexo kinase?

A

Electrophoresis

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14
Q

How can a competitive inhibitor be stopped?

A

By diluting the solution with the substrate

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15
Q

Allosteric effectors are examples of what types of inhibitors?

A

Non-competitive inhibitors

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16
Q

What 3 things make up the amino acid structure?

A

Amino group
Carboxylic acid group
Side chain

17
Q

What does an asymmetric central carbon allow the formation of?

A

Mirror images (enantiomers)

18
Q

What is the primary structure of a protein classed as?

A

The sequence of amino acids in a polypeptide chain

19
Q

What is the secondary structure of a protein described as?

A

Spatial arrangement of amino acid residues that are near each other in the linear sequence

20
Q

Where are the H bonds situated in a beta pleated sheet?

A

Between the amid groups of linear polypeptide chains

21
Q

Does porin have a beta pleated sheet?

22
Q

What is the tertiary structure of a protein described as?

A

The spatial arrangement of amino acid residues that are far apart in a linear sequence

23
Q

Where do ionic interactions take place in a protein?

A

Between 2 close, oppositely charged R groups

24
Q

Disulphide bridges are between what 2 things in a protein?

A

Cysteine residues

25
Where are disulphide bridges common?
Extra-cellular proteins
26
What protein structure does chymotrypsin have?
Tertiary
27
What is the quartenary structure of a protein?
Spatial arrangement of individual polypeptide chains in a multi-subunit protein
28
What remains the same after a protein has been denatured?
The primary structure of a protein
29
Why does the primary structure of a protein remain the same after protein denaturation?
Denaturation reactions are not strong enough to break the peptide bonds
30
What is protein structure dependent on?
DNA sequence coding for amino acids
31
What are glycoproteins composed of?
Protein and carbohydrate
32
What is an example of a glycoprotein?
Immunoglobulin
33
Glycosylation is a process that occurs where?
Endoplasmic reticulum | Golgi apparatus
34
What is the function of a lipoprotein?
Transport water-insoluble fats and cholesterol in the blood
35
What is a metalloprotein?
Protein molecule with a bound metal ion
36
Which part of a haemoglobin chain binds the oxygen molecule?
The Haem group at the centre
37
What type of protein is collagen?
Fibrous protein
38
What type of protein is a LDL receptor?
Glycoprotein