BGM1002/L01 Proteins Overview Flashcards

(43 cards)

1
Q

Why are proteins studied?

A

To understand how cells work.

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2
Q

Give 2 examples of proteins in Medicine.

A

Herceptin - anticancer antibody
Insulin - protein hormone used to treat T1 Diabetes

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3
Q

What is the active/targeted component in most vaccines?

A

Proteins

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4
Q

In a 75kg human, what is the approximate protein weight?

A

Wet - 12kg
Dry - 25%

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5
Q

Approximately what percentage of cell material is protein?

A

50%

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6
Q

What percentage of protein in the body is muscle?

A

50-75%

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7
Q

What structures can proteins form? (Give 5)

A

Cytoskeleton
Enzymes
Cell receptors
Toxins
Antibodies
Hair
Fingernails
Histones
Transporters
Ribosomal proteins
DNA/RNA polymerase

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8
Q

How many different varieties of protein are in the human body?

A

Approximately 20,000.

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9
Q

How many biogenic amino acids are there?

A

20/21

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10
Q

How many levels of protein structure are there? Name them.

A

4 - Primary, secondary, tertiary, quaternary.

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11
Q

What is the relationship between all proteinogenic amino acids?

A

They are L-isomers

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12
Q

Name the 6 common aliphatic amino acids.

A

Alanine, Glycine, Isoeucine, Leucine, Proline, Valine.

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13
Q

Name the 3 common aromatic amino acids.

A

Phenylalanine, Tryptophan, Tyrosine.

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14
Q

Name the 2 common acidic amino acids.

A

Aspartic acid, Glutamic acid.

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15
Q

Name the 3 common basic amino acids.

A

Arginine, Histidine, Lysine

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16
Q

Name the 2 common hydroxylic amino aids.

A

Serine, Threonine.

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17
Q

Name the 2 common Sulfur-containing amino acids.

A

Cysteine, Methionine.

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18
Q

Name the 2 common amidic amino acids.

A

Asparagine, Glutamine.

19
Q

What type of reaction occurs during formation of a peptide bond?

A

Condensation.

20
Q

Which parts of the amino acids react during formation of a peptide bond?

A

Carboxylic acid and amino groups.

21
Q

What type of isomerisation can a peptide bond undergo?

22
Q

What unit of measurement is used for a C-N peptide bond and what is it equal to?

A

Å (angstrom = 0.1 nm)

23
Q

In which way is the polypeptide backbone directional?

A

N-term to C-term.

24
Q

Which organelle synthesises proteins?

25
What type of amino acids do ribosomal proteins have exclusively?
L-amino acids.
26
What type of amino acids are found in some non-ribosomal proteins? Give one example.
D-amino acids - bacterial cell walls.
27
What is a covalent bond?
The strongest molecular bond of two atoms sharing pairs of valence electrons.
28
What are ribosomes composed of?
Large and small sub-units.
29
How do ribosomes catalyse formation of peptide bonds?
By binding mRNA and charged tRNA molecules.
30
What are amino acids delivered to the ribosomes by?
tRNA
31
What occurs as a result of stopping peptide bond formation? Why is this useful?
It stops protein synthesis and kills the cell. It is useful as a drug target.
32
What is a proteome?
The sum of all the proteins in a cell.
33
How are proteins modified after translation?
Post-translational modification.
34
What is a primary protein?
A single linear string of amino acids
35
What is a secondary protein?
A folded 'backbone' of amino acids, in a regular arrangement
36
What is a tertiary protein?
Overall 3-dimensional arrangement of bonded amino acids
37
What is a quaternary protein?
A globular or fibrous structure with multiple strings of protein; a functional arrangement with other proteins or cofactors
38
What is the CORN law?
A rule used to distinguish enantiomers from each other (whether an amino acid is an L-isomer or D-isomer).
39
Which way is a protein read?
From the amino group to the carboxyl group
40
What type of bond is a peptide bond?
Planar bond
41
Which type of bond is the strongest of all molecular bonds?
Covalent bond (shared pairs of valence electrons)
42
What effect does a mutation in the genome have on the resultant protein/amino acid?
It creates a variant protein/different amino acid
43
What type of bodily response can occur due to spike proteins?
Autoimmune response