LECTURE 3: Amino Acids & Proteins Flashcards

1
Q

How many substituents does the alpha-carbon atom have and what does that make it?

A

4 & Chiral

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2
Q

What determines the identity and properties of the amino acid?

A

The R group

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3
Q

All amino acids have mirror images, except which one? EXPLAIN WHY

A

Glycine - it is the only one that does not have a chiral centre, and therefore, it lacks stereoisomers or mirror images.

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4
Q

What form are the amino acids in proteins in? (chirality)

A

L (laevus) form

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5
Q

What form are the amino acids in bacterial cell walls in? (chirality)

A

D (dexter) form

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6
Q

Best unit for expressing acid strength

A

pKa

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7
Q

Higher pKa means

A

smaller Ka and weaker acid

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8
Q

Lower pKa means

A

higher Ka

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9
Q

Carboxyl group in zwitterion

A

Carboxyl group is deprotonated, COO-

pKa= 3.1

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10
Q

Amino group in zwitterion

A

Amino group is deprotonated, NH3+

pKa=8.0

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11
Q

What is a zwitterion

A

amino acids in solution at a neutral pH (7.0) exist predominantly as dipolar ions called zwitterions.

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12
Q

Glycine, Gly, G

A
  • R-group is -H
  • shows no chirality
    -provides flexibility to proteins where other side chains would be too bulky
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13
Q

Alanine, Ala, A

A
  • R group is -CH3
  • aliphatic side chain
  • small size, no reactivity
  • non-polar
  • hydrophobic
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14
Q

Proline, Pro, P

A
  • pyrrolidine ring
  • imposes tight restraints on the conformation of the protein
  • found in proteins that need to be rigid e.g. collagen, and in turns of globular proteins.
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15
Q

Serine, Ser, S

A
  • R group is -CH2-OH
  • hydroxyl functional group
  • polar due to electronegativity values between O and H
  • hydrophilic
  • often found in active sites of enzymes
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16
Q

Histidine, His, H

A
  • R group imidazole ring
  • pKa 6.7, can be neutral or positively charged
  • found in active site of enzymes
17
Q

What is an imidazole ring?

A

A five-membered aromatic ring

18
Q

Cysteine, Cys, C

A
  • R group is -CH2-SH
  • thiol functional group
  • hydrophobic amino acid
  • pKa of 8.4
19
Q

Positively charged R group amino acids

A

Arginine
Lysine
Histidine

20
Q

Hydrophobic amino acids with non-polar R groups

A

Glycine
Alanine
Valine
Cysteine
Proline
Leucine
Isoleucine
Methionine
Tryptophan
Phenylalanine

21
Q

Polar amino acids with neutral R groups

A

Serine
Threonine
Tyrosine
Asparagine
Glutamine

22
Q

Negatively charged R groups

A

Aspartate
Glutamate

23
Q

Residue

A

Each amino acid unit within a polypeptide

24
Q

N-terminal

A

Amino acid sequences are written starting with the amino acid terminal residue

25
Q

C-terminal

A

End of amino acid sequence

26
Q

Purines

A

Adenine and guanine
- bigger looking structure

27
Q

Pyrimidines

A

Cytosine, thymine and uracil
- singular looking structure

28
Q

What type of inhibitor is PALA

A

competitive inhibitor