Intro to Amino Acids and Proteins Flashcards

1
Q

What is the primary structure of proteins?

A

The sequence of amino acids (chain)

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2
Q

What is the center carbon of an amino acid called?

A

Alpha carbon

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3
Q

Carbons that are bonded to 4 different substituent groups are called what?

A

Chiral or assymetric

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4
Q

The alpha carbon is chiral in all amino acids except which one?

A

Glycine

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5
Q

Where are the D-amino acids found?

A

Usually in the cell walls of bacteria - they are an exception to the rule

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6
Q

What are the naturally occurring amino acids?

A

L-amino acids

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7
Q

What is a Zwitterion?

A

Has no overall charge, but regions with positive and negative charges

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8
Q

What are the 9 essential amino acids?

A
Histidine
Isoleucine
Leucine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
Lysine
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9
Q

What are the 7 conditionally non-essential amino acids?

A
Arginine
Asparagine
Glutamine
Glycine
Proline
Serine
Tyrosine
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10
Q

What are the 4 non-essential amino acids?

A

Alanine
Aspartate
Cysteine
Glutamate

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11
Q

When are conditionally non-essential amino acids required?

A
  • Certain stages of growth

- Needed by some people who cannot synthesize them due to a genetic or medical condition

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12
Q

How many nonpolar, aliphatic amino acids are there?

A

7

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13
Q

How many polar, uncharged amino acids are there?

A

5

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14
Q

How many aromatic amino acids are there?

A

3

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15
Q

How many positively charged (basic) amino acids are there?

A

3

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16
Q

How many negatively charged (acidic) amino acids are there?

A

2

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17
Q

What are the 7 nonpolar, aliphatic amino acids?

A
Glycine (Gly, G)
Alanine (Ala, A)
Proline (Pro, P)
Leucine (leu, L)
Isoleucine (Ile, I)
Valine (Val, V)
Methionine (Met, M)
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18
Q

For which type of protein interactions are the nonpolar amino acids important?

A

Hydrophobic protein interactions

19
Q

Which nonpolar amino acid allows for structural flexibility, due to its small size?

A

Glycine (Gly, G)

20
Q

Which nonpolar amino acid reduces flexibility because of its secondary amino group ring structure?

A

Proline (Pro, P)

21
Q

Why is methionine important?

A

It is important in methyl group transfers

22
Q

Is proline flexible or rigid?

A

Rigid

23
Q

What are the 5 polar, uncharged amino acids?

A
Serine (Ser, S)
Threonine (Thr, T)
Cysteine (Cys, C)
Asparagine (Asn, N)
Glutamine (Gln, Q)
24
Q

What makes serine and threonine polar?

A

The OH groups

25
Q

What makes cysteine polar?

A

The sulfur atom

26
Q

What makes asparagine and glutamine polar?

A

The amide groups

27
Q

The polar, uncharged amino acids can form what bonds with water, making them hydrophilic?

A

Hydrogen bonds

28
Q

What are the 3 important functions of the polar, uncharged amino acids?

A
  1. OH of serine and threonine are sites for covalent modifications (ex. physphorylation)
  2. Cysteine forms covalent disulfide bonds that are important form protein folding
  3. Asparagine and glutamine are important N donors/carriers
29
Q

What does oxidizing 2 amino acids allow to bond?

A

It allows bonding between the 2 sulfur atoms

30
Q

What are the 3 aromatic amino acids?

A

Phenylalanine (Phe, F)
Tyrosine (Tyr, Y)
Tryptophan (Trp, W)

31
Q

Are aromatic amino acids relatively polar or nonpolar?

A

Relatively nonpolar - they can participate in hydrophobic interactions

32
Q

At what wavelength do aromatic amino acids absorb light?

A

280 nm - can be used for protein quantitation

33
Q

What are the 3 positively charged (basic) amino acids?

A

Histidine (His, H)
Arginine (Arg, R)
Lysine (Lys, K)

34
Q

Why are the positively charged amino acids positively charged at pH 7?

A

Because of their amino group (NH3+)

35
Q

What are the 2 negatively charged (acidic) amino acids?

A

Aspartate (Asp, D)

Glutamate (Glu, E)

36
Q

Why are the negatively charged amino acids negatively charged at pH 7?

A

Their carboxyl group (COO-) side chains

37
Q

What is desmosine made of?

A

4 lysine residues

38
Q

What does desmosine do?

A

Contributes to the stretchiness of elastin

39
Q

Scurvy is caused by what?

A

A lack of vitamin C

40
Q

Vitamin C is a cofactor for what?

A

Prolyl hydroxylase

41
Q

What does prolyl hydroxylase do?

A

Catalyzes the formation of hydroxyproline, which stabilized collagen

42
Q

Which non-standard amino acid is found in myosin?

A

N-methyllysine

43
Q

Which non-standard amino acid is found in prothrombin?

A

gamma-carboxyglutamate