Lecture 4 Flashcards

Building blocks of proteins

1
Q

How many different amino acids are there?

A

20

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2
Q

What do amino acids contain?

A

Basic amino group, acidic carboxyl group

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3
Q

The alpha carbon of an amino acid is a…?

A

Chiral compound

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4
Q

Define chirality

A

Non-superimposable mirror images on a compound

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5
Q

Amino acids act as __ in solution

A

Zwitterions

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6
Q

Define a zwitterion

A

An ion existing with a +ve and -ve charge at the same time

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7
Q

Amino acids differ by…?

A

Their side chain (R group)

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8
Q

What are the four classes of amino acid?

A

Non-polar, Polar uncharged, Polar positive, Polar negative

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9
Q

What is the water associated nature structure of most proteins?

A

Hydrophobic (non-polar) group gets buried within the core in order to stabilise the protein. Hydrophilic (polar) group lies on the exterior

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10
Q

Why is the hydrophilic component of a protein generally exposed?

A

It requires energy to bury a charge. It is tied up with salt links and H-bonds as well as residues of oppositely charged residues to neutralise the charge

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11
Q

What is different about glycine?

A

It is not chiral as it’s side chain is a singular H, this makes is relatively flexible

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12
Q

What is different about Proline?

A

Side chain bonds back to the main chain N forming an imino acid which is much more rigid

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13
Q

What are the name forms that amino acids exist as?

A

three and one letter abbreviations

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14
Q

Why are one letter abbreviations useful?

A

Helps to describe sequence alignment and mutations

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15
Q

What does ‘E6V’ mean?

A

There is a mutation of glutamate to a valine at position 6 in the protein sequence

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16
Q

What amino acids can act as acids and bases?

A

Amino acids with ionisable side chains where a proton can be donated or accepted

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17
Q

What is pKa

A

the pH at which the group is 50% ionised

18
Q

What is pL

A

the pH at which the net charge on a amino acid is zero (isoelectric point)

19
Q

What is the general pKa values for the carboxyl and amino groups respectively?

A

~2 and ~10

20
Q

What are modified amino acids?

A

Amino acid derivatives that are created in-house

21
Q

What is translation?

A

The translation of RNA to proteins at the ribosome

22
Q

What is ‘post-translational modification’

A

When the amino acid is modified after they are added to a protein

23
Q

What is an example of post-translational modification?

A

The disulphide bond

24
Q

What are some other amino acid modifications?

A

Phosphorylation, hydroxylation, carboxylation, metal binding, iodination, glycosylation

25
What is phosphorylation?
Addition of phosphate or phosphate containing group
26
What is phosphorylation used for?
To control enzyme activity (ON/OFF switch)
27
What is hydroxylation used for?
needed to prevent connective tissue diseases and scurvy (often proline and lysine involved)
28
What is carboxylation used for?
blood clotting (often glutamate)
29
What is glycosylation?
Addition of sugars
30
What is the peptide bond?
The covalent bond between amino acids to form chains of peptides / proteins
31
What occurs when the peptide bond is formed?
Carxoyl - amino water is removed leaving a 'residue'
32
What is the shape of the peptide bond?
Planar
33
Why is the peptide bond planar?
maximised pi bonding overlap
34
What is the bond order character of a peptide bond?
40% double bond
35
What is the rotational barrier of a peptide bond?
~80kJ/mol
36
What creates the dipole in a peptide bond?
The C=O which is partial -ve and N-H which is partial +ve
37
What is a peptide?
A short stretch of amino acids joined by peptide bonds
38
What is a protein
A longer chain of amino acids joined together by peptide bonds, usually with a biological function
39
What are peptides or proteins constructed of?
Amino acid residues
40
What is the purpose of the side chain?
To determine and carry out protein function