Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Enzymology and immunology > MCQ October 22 > Flashcards

MCQ October 22 Flashcards

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What happens to biopharmaceuticals?

A

They are synthesised and genetically modified

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What does a peptide bond do?

A

It joins one amino acid to another

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Name some hydrophobic non polar R groups

A

Proline, glycine and Alanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Name some Polar Uncharged R groups (Hydrophillic)

A

Serine, Cysteine,Tyrosine and Glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Name the two classes of proteins

A

Globular and filamentous

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What are globular proteins?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are filamentous proteins

A

Stable, tough stringy molecules that are insoluble in aqueous solutions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Name some structural functions of filamentous proteins

A

skin, cartilage, teeth

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How many polypeptide chains make up a Quaternary protein

A

more than 1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the four levels of organisation of globular proteins?

A

Primary, Secondary, Tertiary and Quaternary.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What structural elements are included in the secondary structure

A

Helices,loops, turns and sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What amino acids are found in A helices

A

Alanine, Leucine,Methionine, Glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

How are tertiary structures formed?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

How are 3D structures (Tertiary) held together

A

They are held together by
Hydrogen bonds, Ionic bonds, Van der waals forces , Hydrophobic interactions and Di-sulphide bridges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is an example of a quaternary structure

A

Haemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What type of cells are preferable for biopharma and why

A

Mammalian cells are preferred as they have are higher in post translational modification compared to bacteria

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What is the difference between Upstream and down stream

A

Upstream processing is protein biosynthesis for mammalian cell culture.
Downstream is protein extraction from producer and purification.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What are enzymes?

A

They are globular proteins and biological catalysts which catalyse reactions within the body

28
Q

What does Globular proteins serve as?

A

They serve as important components of enzymes,hormones and antibodies

29
Q

What do enzymes convert?

A

Enzymes convert substrates into products

30
Q

In biopharma industry, what do enzymes do?

A

Enzymes accelerates the reaction by lowering the activation energy of a reaction
They dont take part in the reaction

31
Q

What form of amino acid is found in proteins

A

L form of zwitterionic molecules

32
Q

How do domains fold?

A

Domains fold independently and joined by random coils

33
Q

What is the respiration process

A

It is the generation of ATP in all living things

34
Q

Where is the most ATP created

A

Lipid oxidation

35
Q

In terms of IGG what do enzymes add?

A

Enzymes add sugar to the FC region

36
Q

Talk about Cox 2 inhibitors

A

Cox 2 inhibitors are inducable

37
Q

How is pain stopped?

A

Pancdobs prevent cox 2 from inhibiting the archeadonic acid which stops pain.
When cox 2 degrades, it takes the drug with it

38
Q

What does cox 2 inhibit?

A

Cox 1 which releases prostoglandins which causes indegestion

39
Q

How does enzymes accelerate a reaction? What is a good example

A

It lowers the activation energy of a reaction a good example is urease

40
Q

What is an active site

A

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
Q

Active site characteristics

A

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
Q

What is the locke and key method?

A

*The active site of the enzyme is complimentary to the shape of the substrate

43
Q

what is the induced fit method

A

The substrate plays a role in determining the final shape of the enzyme making it partially flexable

44
Q

Name the 4 types of specificity in enzymes

A

Bond specificity
Group specificity
Optical/stereo specificity
Dual specificity

45
Q

What is bond specificity?

A

When an enzyme only reacts with a specific chemical bond

46
Q

What is Group specificity?

A

When an enzyme will only react to substrates with similar functional groups

47
Q

What is optical/stereo specificity?

A

When the enzyme is not specific to substrate but also optical configuration

48
Q

What is dual specificity?

A

Can convert two substrates at once, may act on one substrate by two different reaction types

49
Q

What is an Apoenzyme?

A

Apoenzyme is an enzymatically inactive protein part of an enzyme, which requires a cofactor for its activity

50
Q

What is a cofactor?

A

Cofactors are non-proteins which assist enzymes in performing
catalytic actions.

51
Q

What can cofactors be?

A

Cations (Metal ions)
Co-enzymes (vitamins)

52
Q

Give three examples of cofactors and the enzyme/protein they code for

A

Zinc = Carbonic hyandrase
Zinc = Alcohol dehydrogenase
Potassium and magnesium = Pyruvate phosphokinase

53
Q

Name a cofactor that is permanently attached

A

Haem in Haemoglobin

54
Q

What are the 6 classes of enzymes based on reaction catalysed

A

Oxidoreductase
Transferases
Hydrolases
Lyases
Isomerases
Ligases

55
Q

What is the reaction carried out in oxidoreductases and Transferases? give an example

A

Oxidoreductases= Transfer of reactions, alcohol dehydrogenase
Transferases = Transfer of C,N or P groups, Hexokinase

56
Q

What is the reaction carried out in hydrolases and Lyases? give an example

A

Hydrolases = Bonds cleavage by adding water, Trypsin
Lyases= Cleavage of the same elements to make a double bond, Pyruvate decarboxylase

57
Q

What is the reaction carried out in Isomerases and Ligases? give an example

A

Isomerases= Forms optical or geometric isomers, Maleate isomerase
Ligases= Hydrolysis of high energy phosphates to form new bonds, pyruvate carboxylase

58
Q

What are Oligomeric enzymes?

A

Each enzyme contains ≥ 2 polypeptide chains

59
Q

What is the most common structural characterisation of enzymes involved in glycolysis

A

Oligomeric enzymes

60
Q

In Ec 1 Oxidoreductase, what does Alcohol dehydrogenase do?

A

It converts primary alcohols to Aldehydes in the presence of a cofactor

61
Q

Define Biopharmaceutical

A

Biopharmaceutical is a therapeutic product created through the genetic manipulation of living things

62
Q

What is the central dogma

A

A critical process central to biophama drug production
DNA -> RNA -> Protein

63
Q

What does Biopharmaceuticals drug product =

A

It = recombinant drug protein

64
Q

What does post translational modification refer to?

A

It refers to the covalent and enzymatic modification of proteins during (or after) protein biosynthesis

65
Q

What is is the most common post translational modification.

A

Phosphorylation

66
Q

What are some advantages to CHO cell lines

A

Can produce high protein
They are genetically stable
Can preform post translational modifications

67
Q

What does A refer to in reaction Catalysed

A

type of reaction

68
Q

What does B refer to in reaction Catalysed

A

What type of substrate

69
Q

What does C refer to in reaction Catalysed

A

precise bond/reaction catalysed

70
Q

What does D refer to in reaction Catalysed

A

Individual reaction

Enzymology and immunology (2 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions