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MCAT: Biochemistry > Chapter 1: Amino Acids, Peptides, and Proteins > Flashcards

Chapter 1: Amino Acids, Peptides, and Proteins Flashcards

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MCAT flashcards
1
Q

What are the two functional groups contained in amino acids?

A
  • Amino group (NH2)

- Carboxyl group (COOH)

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2
Q

What is attached to the alpha carbon? (4)

A
  • Amino group (NH2)
  • Carboxyl group (COOH)
  • Hydrogen
  • Side chain (R group)
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3
Q

Do amino acids need to have both the amino and carboxyl groups bonded to the same carbon?

A

No

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4
Q

What are proteinogenic amino acids?

A

The 20 amino acids encoded by the human genetic code

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5
Q

Which amino acid is the only achiral one?

A

Glycine

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6
Q

Are all amino acids optically active?

A

Yes, except glycine

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7
Q

Are amino acids used in eukaryotes L or R?

A

L-amino acids

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8
Q

Which amino acids have an S absolute configuration? Which has an R configuration?

A

S: almost all chiral amino acids
R: cysteine

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9
Q

Which amino acids make up the nonpolar, nonaromatic side chains? (7)

A

Glycine, alanine, valine, leucine, isolucine, methionine, proline

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10
Q

Which amino acid is a cyclic amino acid? How many members does its ring have?

A
  • Proline

- 5-membered ring

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11
Q

Which amino acids make up the aromatic side chains? (3)

A

Phenylalanine, tryptophan, tyrosine

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12
Q

Which amino acids contain an OH group?

A

Tyrosine, serine, threonine

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13
Q

Which amino acids make up the polar side chains? (5)

A

Serine, threonine, asparagine, glutamine, cysteine

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14
Q

In which amino acids do amide nitrogens NOT gain or lose protons with changes in pH?

A

Asparagine and glutamine

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15
Q

Which amino acid has a thiol group? What is a thiol group?

A
  • SH

- Cysteine

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16
Q

Which amino acids make up the negatively charged (acidic) side chains?

A

Aspartic acid (aspartate) and glutamic acid (glutamate)

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17
Q

What is physiological pH?

A

7.4

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18
Q

What is the difference between aspartate and aspartic acid?

A

Aspartate is the deprotonated form of aspartic acid

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19
Q

Which amino acids make up the positively charged (basic) side chains?

A

Lysine, arginine, histidine

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20
Q

Which amino acid has an imidazole ring?

A

Histidine

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21
Q

When is histidine protonated?

A

When pH < pKa (around 6), the nitrogen atom can become protonated

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22
Q

Classifying amino acids as hydrophobic and hydrophilic is complex. Which amino acids are definitely hydrophobic? Where would they be found?

A
  • Long alkyl side chains: alanine, isoleucine, leucine, valine, and phenylalanine
  • Found in the interior of proteins
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23
Q

Classifying amino acids as hydrophobic and hydrophilic is complex. Which amino acids are definitely hydrophilic? Where would they be found?

A
  • Charged side chains
  • Amides: asparagine and glutamine
  • Found in the surface of proteins, in contact with water
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24
Q

Define amphoteric species. Give an example.

A

They can accept or donate protons (ex: amino acids)

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25
Q

How do ionizable groups tend to react under acidic conditions? What about under basic conditions?

A

Acidic: gain protons (protonation)
Basic: lose protons (deprotonation)

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26
Q

What is the pKa? What is the concentration of HA equivalent to?

A

The pH at which half of the species is deprotonated

HA) = (A-

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27
Q

If the pH is below the pKa, what will happen? If the pH is above the pKa, what will happen?

A

pH < pKa: protonation

pH > pKa: deprotonation

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28
Q

What is pKa1? What is pKa2?

A

pKa1: pKa for the carboxyl group
pKa2: pKa for the amino group

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29
Q

How many pKas are there for amino acids?

A
  • 2 if there is no ionizable side chain

- 3 if there is an ionizable side chain

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30
Q

What is the overall charge of amino acids under acidic conditions (assuming no ionizable side chains)?

A

+1 (fully protonated)

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31
Q

What is the overall charge of amino acids under basic conditions (assuming no ionizable side chains)?

A

-1 (fully deprotonated)

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32
Q

How is the amino acid when the pH is near the pI of the amino acid?

A

Neutral zwitterion

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33
Q

Define zwitterions. What are they also called?

A
  • Dipolar ions

- Has both a positive and negative charge

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34
Q

What is the equation to calculate the pI of a neutral amino acid?

A

(pKa (NH3+ group) + pKa (COOH group)) / 2

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35
Q

What is the pH equal to when the concentrations of a fully protonated amino acids are equal to its zwitterion? How many equivalents of base needed to be added?

A
  • pH = pKa1

- 0.5 equivalents of base

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36
Q

What is the optimal buffering point? What is the buffering region?

A

pH = pKa

pKa +/- 1

37
Q

What is the isoelectric point (pI)? How many equivalents of base needed to be added to reach this point?

A
  • The pH at which the molecule is electrically neutral

- 1 equivalent of base

38
Q

What is the pH equal to when the concentration of the zwitterion form equals the concentration of the fully deprotonated form? How many equivalents of base needed to be added?

A
  • pH = pKa2

- 1.5 equivalents of base

39
Q

How much base equivalents need to be added to fully protonate an amino acid?

A

2 equivalents of base

40
Q

How can you calculate the pI of an acidic amino acid?

A

(pKa (R group) + pKa (COOH group)) / 2

41
Q

How can you calculate the pI of a basic amino acid?

A

(pKa (NH3+ group) + pKa (R group)) / 2

42
Q

How do the pI values compare between acidic side chains and basic side chains?

A

Acidic side chains: below 6

Basic side chains: above 6

43
Q

How many resides are contained in oligopeptides? What about polypeptides?

A

Oligopeptides: 3-20
Polypeptides: more than 20

44
Q

A peptide bond forms between the ____ group of one amino acid and the ____ group of another amino acid.

A

–COO- and NH3+

45
Q

What kind of reaction drives peptide bond formation?

A

Condensation/Dehydration: loss of water

46
Q

How is a peptide bond formed?

A
  • Electrophilic carbonyl carbon on AA1 is attacked by the nucleophilic amino group on AA2
  • After, the hydroxyl group of the carboxylic acid is kicked off
  • Result: formation of a peptide bond
47
Q

Why do amide groups exhibit resonance?

A

Delocalizable pi electrons in the carbonyl and in the lone pair on the amino nitrogen

48
Q

What does the resonance of amide groups cause?

A

The C-N bond in the amide has a partial bond character

49
Q

In what order are peptides drawn in?

A

In the same order that it is synthesized by ribosomes: from the N-terminus to the C-terminus

50
Q

What is the result of the partial bond character in the C-N bond of a peptide?

A

Rotation of the protein backbone around its C-N amide bond is restricted

51
Q

Give examples of hydrolytic enzymes.

A

Trypsin and chymotrypsin

52
Q

Where does trypsin cleave?

A

At the carboxyl end of arginine and lysine

53
Q

Where does chymotrypsin cleave?

A

At the carboxyl end of phenylalanine, tryptophan, and tyrosine

54
Q

How do hydrolytic enzymes break apart the amide bond?

A

By adding a hydrogen atom to the amide nitrogen and an OH group to the carbonyl carbon

55
Q

Define primary structure.

A

Linear sequence of amino acids in chain

56
Q

Define secondary structure.

A

Local structure determined by nearby amino acids

57
Q

Define tertiary structure.

A

Three-dimensional shape of protein

58
Q

Define quaternary structure.

A

Interaction between separate subunits of a multisubunit protein

59
Q

What is the stabilizing bond of primary structure?

A

Peptide (amide) bonds

60
Q

What is the stabilizing bond of secondary structure?

A

Hydrogen bonds

61
Q

What is the stabilizing bond of tertiary and quaternary structures?

A

van der Waals forces, hydrogen bonds, ionic bonds, covalent bonds

62
Q

What are the subtypes of secondary structure? (2)

A
  • a-helix

- B-pleated sheet

63
Q

What are the subtypes of tertiary structure? (3)

A
  • Hydrophobic interactions
  • Acid-base/salt bridges
  • Disulfide links
64
Q

How can the primary structure of a protein be determined in a laboratory setting?

A

Through sequencing

65
Q

Do the peptide chains in an a-helix coil clockwise or counter clockwise?

A

Clockwise

66
Q

The a-helix is stabilized by intramolecular hydrogen bonds between a ________ atom and an ______ atom _ residues down the chain

A
  • Carbonyl oxygen
  • Amide hydrogen
  • 4 residues
67
Q

The a-helix is an important component in which structure?

A

Keratin

68
Q

Where is proline found/not found in secondary structures?

A

Found: turns between chains of a B-pleated sheet
Not found: middle of pleated sheets or a-helices
* Creates kinks in a-helices and turns in B-sheets

69
Q

_____, the primary protein component of silk fibres, is composed of B-pleated sheets

A

Fibroin

70
Q

How can proteins be broadly divided?

A

Fibrous proteins (collagen) and globular proteins (myoglobin)

71
Q

How do disulfide bonds form?

A

When two cysteine molecules become oxidized to form cystine

72
Q

What do disulfide bonds create in the protein chain?

A

Loops

73
Q

What does forming a disulfide bond require?

A

The loss of two protons and two electrons (oxidation)

74
Q

What are molten globules?

A

The intermediate state between secondary and tertiary structures

75
Q

What is denaturation?

A

The loss of a protein’s tertiary structure, which makes it lose its function

76
Q

What explains hydrophobic folding?

A

Increases entropy by allowing water molecules on the surface of the protein to have more possible positions and configurations (positive deltaS, deltaG <0, stabilizes the protein)

77
Q

Do all proteins have tertiary structure? What about quaternary structure?

A

Tertiary: yes
Quaternary: no

78
Q

What are the 4 roles of quaternary structures?

A

1) Be more stable (reducing the surface area of the protein complex)
2) Reduce the amount of DNA needed to encode the protein complex
3) Bring catalytic sites together
4) Induce cooperativity or allosteric effects

79
Q

What are conjugated proteins?

A

Proteins with covalently attached molecules

80
Q

What is the attached molecule on a conjugated protein called? What can it be?

A
  • Prosthetic group

- Metal ion, vitamin, lipid, carbohydrate, or nucleic acid

81
Q

What is the prosthetic group in hemoglobin’s subunits?

A

Heme (contains an iron atom in its core)

82
Q

What denatures proteins? (2)

A
  • Heat

- Solutes

83
Q

Why does heat denature proteins?

A

By increasing their average kinetic energy, thus disrupting hydrophobic interactions

84
Q

Why do solutes denature proteins?

A

By disrupting elements of secondary, tertiary, and quaternary structure

85
Q

How many distinct tripeptides can be formed from three amino acids?

A

3 x 2 x 1 = 6

86
Q

Which amino acids are likely to be found in a transmembrane portion of an a-helix?

A

Hydrophobic amino acids

87
Q

Which two amino acids have chiral carbons in their side chains?

A

Threonine and isoleucine

88
Q

Which amino acid is likely to be found in high concentrations in collagen?

A

Glycine

MCAT: Biochemistry (12 decks)

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