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Enzymology and immunology > MCQ October 22 > Flashcards

MCQ October 22 Flashcards

(72 cards)

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1
Q

Give examples of biopharmaceuticals and what is it

A

Biopharmaceuticals are recombinant proteins. The drug product is derived from the protein
e.g hormones,MAB,Enzymes, cytokines

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2
Q

What is the number 1 product made by biopharma industry and how does it work

A

Monoclonal antibodies. They target only one epitope on antigens

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3
Q

What happens to biopharmaceuticals?

A

They are synthesised and genetically modified

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3
Q

What is the backbone Structure of a Polypeptide

A

An amino group
A chiral carbon attached to an R group and a H
A carboxyl group

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4
Q

List some properties of a peptide bond

A

It has partial double bond characteristics, its planar and no rotation around the peptide bond

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4
Q

What does a peptide bond do?

A

It joins one amino acid to another

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5
Q

Name some hydrophobic non polar R groups

A

Proline, glycine and Alanine

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6
Q

Name some Polar Uncharged R groups (Hydrophillic)

A

Serine, Cysteine,Tyrosine and Glutamine

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7
Q

How many amino acids does oligopeptides, polypeptides and proteins have?

A

Oligopeptides = up to 25
Polypeptides = more than 25
Proteins= more than 100

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8
Q

Give some characteristics of proteins

A

Most abundant macromolecule found within cells

Consist of the elements C, H, O and N.
Polymers of amino acids with large molecular weights

Different amino acids determine the overall chemical and structural properties of a protein.

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9
Q

Name the two classes of proteins

A

Globular and filamentous

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10
Q

What are globular proteins?

A

They are unstable, compact molecules that are soluble in aqueous solutions

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11
Q

What are filamentous proteins

A

Stable, tough stringy molecules that are insoluble in aqueous solutions

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12
Q

Name some structural functions of filamentous proteins

A

skin, cartilage, teeth

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13
Q

How many polypeptide chains make up a Quaternary protein

A

more than 1

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14
Q

What are the four levels of organisation of globular proteins?

A

Primary, Secondary, Tertiary and Quaternary.

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15
Q

What does the primary structure do and what does it include?

A

It includes insulin and it gives important information about the properties of the proteins from the number, type and sequence of amino acids.

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16
Q

In the primary structure, what does lots of hydrophobic amino acids mean?

A

It means it will not be soluble in an aqueous environment making it hydrophobic

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17
Q

What structural elements are included in the secondary structure

A

Helices,loops, turns and sheets

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18
Q

What stabilises the alpha helix?

A

A regular pattern of H bonds and every backbone C=O group H bonds to an N-H group

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19
Q

What amino acids are found in A helices

A

Alanine, Leucine,Methionine, Glutamate

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20
Q

What is the make up of Beta pleated sheets?

A

5-10 amino acid residues in length
Extended zigzag conformation
Two or more strands align to make the sheets
Held together by beta pleated sheets

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21
Q

What are the differences between parallel and and antiparallel beta pleated sheets

A

With antiparallel the polypeptide chains are in opposite directions and connected via hairpin loops

Parallel, the chains are stacked in the same directions and are connected via crossover loops

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22
Q

How are tertiary structures formed?

A

They are formed after the assembly of structural elements joined by coils and hairpin loops

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23
How are 3D structures (Tertiary) held together
They are held together by Hydrogen bonds, Ionic bonds, Van der waals forces , Hydrophobic interactions and Di-sulphide bridges
24
What is an example of a quaternary structure
Haemoglobin
25
What type of cells are preferable for biopharma and why
Mammalian cells are preferred as they have are higher in post translational modification compared to bacteria
26
What is the difference between Upstream and down stream
Upstream processing is protein biosynthesis for mammalian cell culture. Downstream is protein extraction from producer and purification.
27
What are enzymes?
They are globular proteins and biological catalysts which catalyse reactions within the body
28
What does Globular proteins serve as?
They serve as important components of enzymes,hormones and antibodies
29
What do enzymes convert?
Enzymes convert substrates into products
30
In biopharma industry, what do enzymes do?
Enzymes accelerates the reaction by lowering the activation energy of a reaction They dont take part in the reaction
31
What form of amino acid is found in proteins
L form of zwitterionic molecules
32
How do domains fold?
Domains fold independently and joined by random coils
33
What is the respiration process
It is the generation of ATP in all living things
34
Where is the most ATP created
Lipid oxidation
35
In terms of IGG what do enzymes add?
Enzymes add sugar to the FC region
36
Talk about Cox 2 inhibitors
Cox 2 inhibitors are inducable
37
How is pain stopped?
Pancdobs prevent cox 2 from inhibiting the archeadonic acid which stops pain. When cox 2 degrades, it takes the drug with it
38
What does cox 2 inhibit?
Cox 1 which releases prostoglandins which causes indegestion
39
How does enzymes accelerate a reaction? What is a good example
It lowers the activation energy of a reaction a good example is urease
40
What is an active site
it is the part of the protein that the substrate binds to Proteins have 3D shapes so an amino acid can bind to it
41
Active site characteristics
Amino acids may be separated from each other Substrate binds to the amino acid via weak bonds i.e hydrogen bonds Enzymes may have more than one substrate
42
What is the locke and key method?
*The active site of the enzyme is complimentary to the shape of the substrate
43
what is the induced fit method
The substrate plays a role in determining the final shape of the enzyme making it partially flexable
44
Name the 4 types of specificity in enzymes
Bond specificity Group specificity Optical/stereo specificity Dual specificity
45
What is bond specificity?
When an enzyme only reacts with a specific chemical bond
46
What is Group specificity?
When an enzyme will only react to substrates with similar functional groups
47
What is optical/stereo specificity?
When the enzyme is not specific to substrate but also optical configuration
48
What is dual specificity?
Can convert two substrates at once, may act on one substrate by two different reaction types
49
What is an Apoenzyme?
Apoenzyme is an enzymatically inactive protein part of an enzyme, which requires a cofactor for its activity
50
What is a cofactor?
Cofactors are non-proteins which assist enzymes in performing catalytic actions.
51
What can cofactors be?
Cations (Metal ions) Co-enzymes (vitamins)
52
Give three examples of cofactors and the enzyme/protein they code for
Zinc = Carbonic hyandrase Zinc = Alcohol dehydrogenase Potassium and magnesium = Pyruvate phosphokinase
53
Name a cofactor that is permanently attached
Haem in Haemoglobin
54
What are the 6 classes of enzymes based on reaction catalysed
Oxidoreductase Transferases Hydrolases Lyases Isomerases Ligases
55
What is the reaction carried out in oxidoreductases and Transferases? give an example
Oxidoreductases= Transfer of reactions, alcohol dehydrogenase Transferases = Transfer of C,N or P groups, Hexokinase
56
What is the reaction carried out in hydrolases and Lyases? give an example
Hydrolases = Bonds cleavage by adding water, Trypsin Lyases= Cleavage of the same elements to make a double bond, Pyruvate decarboxylase
57
What is the reaction carried out in Isomerases and Ligases? give an example
Isomerases= Forms optical or geometric isomers, Maleate isomerase Ligases= Hydrolysis of high energy phosphates to form new bonds, pyruvate carboxylase
58
What are Oligomeric enzymes?
Each enzyme contains ≥ 2 polypeptide chains
59
What is the most common structural characterisation of enzymes involved in glycolysis
Oligomeric enzymes
60
In Ec 1 Oxidoreductase, what does Alcohol dehydrogenase do?
It converts primary alcohols to Aldehydes in the presence of a cofactor
61
Define Biopharmaceutical
Biopharmaceutical is a therapeutic product created through the genetic manipulation of living things
62
What is the central dogma
A critical process central to biophama drug production DNA -> RNA -> Protein
63
What does Biopharmaceuticals drug product =
It = recombinant drug protein
64
What does post translational modification refer to?
It refers to the covalent and enzymatic modification of proteins during (or after) protein biosynthesis
65
What is is the most common post translational modification.
Phosphorylation
66
What are some advantages to CHO cell lines
Can produce high protein They are genetically stable Can preform post translational modifications
67
What does A refer to in reaction Catalysed
type of reaction
68
What does B refer to in reaction Catalysed
What type of substrate
69
What does C refer to in reaction Catalysed
precise bond/reaction catalysed
70
What does D refer to in reaction Catalysed
Individual reaction

Enzymology and immunology (3 decks)

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