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Science for Medicine > Proteins and Enzymes > Flashcards

Proteins and Enzymes Flashcards

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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?

A

Yes

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
Q

Where are disulphide bridges common?

A

Extra-cellular proteins

26
Q

What protein structure does chymotrypsin have?

A

Tertiary

27
Q

What is the quartenary structure of a protein?

A

Spatial arrangement of individual polypeptide chains in a multi-subunit protein

28
Q

What remains the same after a protein has been denatured?

A

The primary structure of a protein

29
Q

Why does the primary structure of a protein remain the same after protein denaturation?

A

Denaturation reactions are not strong enough to break the peptide bonds

30
Q

What is protein structure dependent on?

A

DNA sequence coding for amino acids

31
Q

What are glycoproteins composed of?

A

Protein and carbohydrate

32
Q

What is an example of a glycoprotein?

A

Immunoglobulin

33
Q

Glycosylation is a process that occurs where?

A

Endoplasmic reticulum

Golgi apparatus

34
Q

What is the function of a lipoprotein?

A

Transport water-insoluble fats and cholesterol in the blood

35
Q

What is a metalloprotein?

A

Protein molecule with a bound metal ion

36
Q

Which part of a haemoglobin chain binds the oxygen molecule?

A

The Haem group at the centre

37
Q

What type of protein is collagen?

A

Fibrous protein

38
Q

What type of protein is a LDL receptor?

A

Glycoprotein

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