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Introductory Biochemistry > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

What are some functions of proteins?

A

Structure, catalysis, communication, transport, movement

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2
Q

What is the monomer of proteins?

A

Amino acids

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3
Q

What 4 groups are attached to the alpha carbon in an amino acid?

A

An amino group, a hydrogen (alpha hydrogen), a carboxyl group, and the side chain

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4
Q

What is a zwitterion?

A

A molecule that contains both positive and negative charges

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5
Q

Which amino acid is the only one that isn’t chiral?

A

Glycine. The side chain is another hydrogen

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6
Q

What system for naming chirality is used for amino acids instead of R and S?

A

L and D

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7
Q

Why is stereochemistry important in biological systems?

A

Especially for enantiomers, the molecule can have all the same chemical and physical properties but will interact with receptors differently

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8
Q

Which stereoisomer of amino acids is the only one typically found in proteins? Where can the other one be found?

A

L. D isomers can be found in peptidoglycan and in metabolism

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9
Q

Which amino acids have hydrophobic side chains? Which ones have aliphatic and aromatic side chains?

A

Alanine, Valine, Leucine, Isoleucine, Proline, Tryptophan, Methionine, Phenylalanine.

Tryptophan and Phenylalanine have aromatic side chains, the rest have aliphatic side chains

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10
Q

Which amino acids have polar side chains? Which ones have aliphatic and aromatic side chains?

A

Serine, Tyrosine, Threonine, Cysteine, Histidine, Asparagine, Glutamine.

Tyrosine and Histidine have aromatic side chains, the rest have aliphatic side chains

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11
Q

Which amino acids have charged side chains (at a neutral pH)? Which ones are positively charged, negatively charged, acidic, and basic?

A

Lysine, Aspartate, Glutamate, Arginine

Lysine and arginine are positively charged and basic, glutamate and aspartate are negatively charged and acidic

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12
Q

What is the 3 letter code, 1 letter code, side chain property for glycine?

A

Gly, G, just a hydrogen

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13
Q

What is the 3 letter code, 1 letter code, side chain property for alanine?

A

Ala, A, hydrophobic aliphatic

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14
Q

What is the 3 letter code, 1 letter code, side chain property for valine?

A

Val, V, hydrophobic aliphatic

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15
Q

What is the 3 letter code, 1 letter code, side chain property for leucine?

A

Leu, L, hydrophobic aliphatic

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16
Q

What is the 3 letter code, 1 letter code, side chain property for isoleucine? What does isoleucine have that valine and leucine don’t have?

A

Ile, I, hydrophobic aliphatic. It has a second chiral centre

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17
Q

What is the 3 letter code, 1 letter code, side chain property for methionine?

A

Met, M, hydrophobic aliphatic

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18
Q

What is the 3 letter code, 1 letter code, side chain property for proline? What side chain feature is unique about proline?

A

Pro, P, hydrophobic aliphatic. The side chain is cyclic and the amino group has one less hydrogen than normal

19
Q

What is the 3 letter code, 1 letter code, side chain property for phenylalanine?

A

Phe, F, hydrophobic aromatic

20
Q

What is the 3 letter code, 1 letter code, side chain property for tryptophan? What is unique about tryptophan?

A

Trp, W, hydrophobic aromatic. It is the bulkiest amino acid and can donate a hydrogen bond even though its non polar

21
Q

What is the 3 letter code, 1 letter code, side chain property for serine?

A

Ser, S, polar aliphatic

22
Q

What is the 3 letter code, 1 letter code, side chain property for threonine? What characteristic does threonine have that serine doesn’t?

A

Thr, T, polar aliphatic. It has a 2nd chiral centre

23
Q

What is the 3 letter code, 1 letter code, side chain property for cysteine? What is cysteine able to do that no other amino acid can do?

A

Cys, C, polar aliphatic. It can form disulfide bridges

24
Q

What is the 3 letter code, 1 letter code, side chain property for asparagine?

A

Asn, N, polar aliphatic

25
What is the 3 letter code, 1 letter code, side chain property for glutamine?
Gln, Q, polar aliphatic
26
What is the 3 letter code, 1 letter code, side chain property for tyrosine?
Tyr, Y, polar aromatic
27
What is the 3 letter code, 1 letter code, side chain property for histidine?
His, H, polar aromatic
28
What is the 3 letter code, 1 letter code, side chain property for lysine?
Lys, K, charged (positive, basic)
29
What is the 3 letter code, 1 letter code, side chain property for arginine?
Arg, R, charged (positive, basic)
30
What is the 3 letter code, 1 letter code, side chain property for aspartate?
Asp, D, charged (negative, acidic)
31
What is the 3 letter code, 1 letter code, side chain property for glutamate?
Glu, E, charged (negative, acidic)
32
How many ionizable groups do amino acids contain?
2 - the amino and the carboxyl. Some have ionizable side chains and have 3 ionizable side chains
33
Why are most amino acids zwitterions at neutral pH?
Without an ionizable side chain, the amino group is in the HA form (-NH3) and the carboxyl group is in the A- form (-COO-)
34
What is the isoelectric point (pI)? How is it calculated?
The pH where the net charge of an ampholyte is 0. Is the average of the two pKa's
35
Which amino acids have ionizable side chains?
Aspartate, glutamate, tyrosine, cysteine, histidine, arginine, lysine
36
Even though they have an ionizable side chain, why aren't tyrosine and cysteine considered to be charged amino acids?
They are in their HA forms at neutral pH so the side chains aren't charged
37
Which amino acids have side chains that can be hydrogen bond donors?
Trp, Ser, Thr, Tyr (HA), Arg, Lys, His, Cys (HA), Asp (HA), Glu (HA), Gln (2), Asn (2)
38
Which amino have side chains that can be hydrogen bond donors?
Ser (2), Thr (2), Tyr, Asn (2), Gln (2), Asp (A-), Glu (A-), Lys (A-), Arg (A-), His (A-)
39
Why can't cysteine accept hydrogen bonds?
The sulfur can't accept hydrogen bonds because the outer electrons have too much energy
40
How are uncommon amino acids produced?
Modification of the side chains of common amino acids through phosphorylation or hydroxylation. They are not made through translation
41
What is hydroxylation? What does the enzyme require for it to function?
The addition of an OH to proline or lysine, which is an irreversible modification. The enzyme requires vitamin C to function
42
Where are hydroxyproline and hydroxylysine found?
Collagen
43
What is phosphorylation?
The addition of a phosphate to a serine, threonine, or tyrosine
44
What enzyme adds phosphates? What enzyme removes phosphates?
Kinases and phosphatases (through hydrolysis)

Introductory Biochemistry (16 decks)

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