MCQ October 22 Flashcards
Give examples of biopharmaceuticals and what is it
Biopharmaceuticals are recombinant proteins. The drug product is derived from the protein
e.g hormones,MAB,Enzymes, cytokines
What is the number 1 product made by biopharma industry and how does it work
Monoclonal antibodies. They target only one epitope on antigens
What happens to biopharmaceuticals?
They are synthesised and genetically modified
What is the backbone Structure of a Polypeptide
An amino group
A chiral carbon attached to an R group and a H
A carboxyl group
List some properties of a peptide bond
It has partial double bond characteristics, its planar and no rotation around the peptide bond
What does a peptide bond do?
It joins one amino acid to another
Name some hydrophobic non polar R groups
Proline, glycine and Alanine
Name some Polar Uncharged R groups (Hydrophillic)
Serine, Cysteine,Tyrosine and Glutamine
How many amino acids does oligopeptides, polypeptides and proteins have?
Oligopeptides = up to 25
Polypeptides = more than 25
Proteins= more than 100
Give some characteristics of proteins
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.
Name the two classes of proteins
Globular and filamentous
What are globular proteins?
They are unstable, compact molecules that are soluble in aqueous solutions
What are filamentous proteins
Stable, tough stringy molecules that are insoluble in aqueous solutions
Name some structural functions of filamentous proteins
skin, cartilage, teeth
How many polypeptide chains make up a Quaternary protein
more than 1
What are the four levels of organisation of globular proteins?
Primary, Secondary, Tertiary and Quaternary.
What does the primary structure do and what does it include?
It includes insulin and it gives important information about the properties of the proteins from the number, type and sequence of amino acids.
In the primary structure, what does lots of hydrophobic amino acids mean?
It means it will not be soluble in an aqueous environment making it hydrophobic
What structural elements are included in the secondary structure
Helices,loops, turns and sheets
What stabilises the alpha helix?
A regular pattern of H bonds and every backbone C=O group H bonds to an N-H group
What amino acids are found in A helices
Alanine, Leucine,Methionine, Glutamate
What is the make up of Beta pleated sheets?
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
What are the differences between parallel and and antiparallel beta pleated sheets
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 are tertiary structures formed?
They are formed after the assembly of structural elements joined by coils and hairpin loops
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
What is an example of a quaternary structure
Haemoglobin
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
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.
What are enzymes?
They are globular proteins and biological catalysts which catalyse reactions within the body
What does Globular proteins serve as?
They serve as important components of enzymes,hormones and antibodies
What do enzymes convert?
Enzymes convert substrates into products
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
What form of amino acid is found in proteins
L form of zwitterionic molecules
How do domains fold?
Domains fold independently and joined by random coils
What is the respiration process
It is the generation of ATP in all living things
Where is the most ATP created
Lipid oxidation
In terms of IGG what do enzymes add?
Enzymes add sugar to the FC region
Talk about Cox 2 inhibitors
Cox 2 inhibitors are inducable
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
What does cox 2 inhibit?
Cox 1 which releases prostoglandins which causes indegestion
How does enzymes accelerate a reaction? What is a good example
It lowers the activation energy of a reaction a good example is urease
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
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
What is the locke and key method?
*The active site of the enzyme is complimentary to the shape of the substrate
what is the induced fit method
The substrate plays a role in determining the final shape of the enzyme making it partially flexable
Name the 4 types of specificity in enzymes
Bond specificity
Group specificity
Optical/stereo specificity
Dual specificity
What is bond specificity?
When an enzyme only reacts with a specific chemical bond
What is Group specificity?
When an enzyme will only react to substrates with similar functional groups
What is optical/stereo specificity?
When the enzyme is not specific to substrate but also optical configuration
What is dual specificity?
Can convert two substrates at once, may act on one substrate by two different reaction types
What is an Apoenzyme?
Apoenzyme is an enzymatically inactive protein part of an enzyme, which requires a cofactor for its activity
What is a cofactor?
Cofactors are non-proteins which assist enzymes in performing
catalytic actions.
What can cofactors be?
Cations (Metal ions)
Co-enzymes (vitamins)
Give three examples of cofactors and the enzyme/protein they code for
Zinc = Carbonic hyandrase
Zinc = Alcohol dehydrogenase
Potassium and magnesium = Pyruvate phosphokinase
Name a cofactor that is permanently attached
Haem in Haemoglobin
What are the 6 classes of enzymes based on reaction catalysed
Oxidoreductase
Transferases
Hydrolases
Lyases
Isomerases
Ligases
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
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
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
What are Oligomeric enzymes?
Each enzyme contains ≥ 2 polypeptide chains
What is the most common structural characterisation of enzymes involved in glycolysis
Oligomeric enzymes
In Ec 1 Oxidoreductase, what does Alcohol dehydrogenase do?
It converts primary alcohols to Aldehydes in the presence of a cofactor
Define Biopharmaceutical
Biopharmaceutical is a therapeutic product created through the genetic manipulation of living things
What is the central dogma
A critical process central to biophama drug production
DNA -> RNA -> Protein
What does Biopharmaceuticals drug product =
It = recombinant drug protein
What does post translational modification refer to?
It refers to the covalent and enzymatic modification of proteins during (or after) protein biosynthesis
What is is the most common post translational modification.
Phosphorylation
What are some advantages to CHO cell lines
Can produce high protein
They are genetically stable
Can preform post translational modifications
What does A refer to in reaction Catalysed
type of reaction
What does B refer to in reaction Catalysed
What type of substrate
What does C refer to in reaction Catalysed
precise bond/reaction catalysed
What does D refer to in reaction Catalysed
Individual reaction
