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MCAT > Amino Acids > Flashcards

Amino Acids Flashcards

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MCAT flashcards
1
Q

Most AAs are found in the R or S configuration? What are the exceptions?

A

Most amino acids are S, except cysteine is R and glycine is achiral

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2
Q

Naturally occuring amino acids that play a major role in our body are all in the D or L configuration? What about carbs?

A

Most are found in the L configuration in eukaryotes and are found in the D configuration in many bacteria while carbs are often found in the D configuration

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3
Q

Which is the simplest amino acid and is achiral?

A

Glycine, Gly, G

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4
Q

Which amino acid has just a methyl group as a side chain and is often used as the conical example of a simple, small, nonpolar AA?

A

Alanine. Ala, A

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5
Q

Which amino acids contain isopropyl groups?

A

Valine, Val, V and Isoleucine, Ile, I

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6
Q

Which amino acid if substituted for glutamic acid in Hb can cause sickle cell disease?

A

Valine, Val, V

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7
Q

Which are the essential amino acid?

A

My tall, handsome, vegan friend is watering kale leaves:

  • Methionine, Met, M
  • Threonine, Thr, T
  • Histidine, His, H
  • Valine, Val, V
  • Phenylalanine, Phe, F
  • Isoleucine, Ile, I
  • Tryptophan, Trp, W
  • Tyrosine, Tyr, K
  • Leucine, Leu, L
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8
Q

What are the two sulfur containing amino acids?

A

Methionine, Met, M and Cysteine, Cys, C

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9
Q

Why is methionine still considered nonpolar?

A

Bc the only bond sulfur makes is to carbon and the electronegativity difference bt S and C is only 0.3, making it the more inert of the two sulfur containing AAs

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10
Q

Which essential amino acid is found in high quantities in eggs?

A

Methionine, Met, M

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11
Q

Which amino acid is involved in angiogenesis and DNA methylation?

A

Methionine, Met, M

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12
Q

What amino acid does the start codon AUG code for?

A

Methionine, Met, M

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13
Q

What is so unique about proline’s structure?

A

It is the only AA that has a cyclic component that links back w the AA itself, so the N in the amine group of the back bone is actually part of the proline side chain

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14
Q

What does proline have the ability to do? How does this determine its locations in proteins?

A
  • It introduces proline kinks, which have the ability to break up secondary structures/ motifs and .: the 3D structures formed by the interactions among the amine and carboxylic acids of the AAs
  • This is why it is rarely found in the middle of secondary structures like alpha- helices and beta- pleated sheets, but instead it is found at the TURNS of beta pleated sheets
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15
Q

What are the aromatic amino acids? Which one is also an alcohol?

A
  • Phenylalanine, tryptophan, and tyrosine

- Tyrosine is also an alcohol

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16
Q

The presence of what must be controlled in phenylketonuria? What is phenylketonuria?

A
  • Phenylalanine, Phe, F

- A congenital malfunction of the enzyme necessary to convert phenylalanine into tyrosine

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17
Q

What is characteristic of tryptophan’s structure?

A

Its 2 ring side chain, which contains a benzene rings and a heterocyclic ring containing an amine group

18
Q

Which AA is a precursor for serotonin and melatonin?

A

Tryptophan

19
Q

Why can tyrosine be considered both polar and nonpolar?

A

It is considered to be amphipathic: The C-OH bond is polar but this is considered to be outweighed by the larger, sterically bulky, hydrophobic ring .: Making the overall behavior more nonpolar. However, the C-OH bond does make it more water soluble than phenylalanine

20
Q

Which AA is a precursor for many biologically relevant signaling molecules like dopamine, epinephrine, and norepinephrine?

A

Tyrosine, Tyr, Y

21
Q

Which AAs contain alcohols making them targets for covalent modifications, ESPECIALLY phosphorylation? Which one is the most commonly phosphorylated?

A
  • Serine, Threonine, and Tyrosine

- Serine, Ser, S

22
Q

Which of the amino acids containing alcohols has a primary alcohol and which has a secondary alcohol?

A

Serine has a primary alcohol and threonine has a secondary alcohol

23
Q

Which amino acids reacts w reducing sugars like fructose and glucose in baked and fried foods to produce the potentially carcinogenic compound, acrylamide?

A

Asparagine, Asn, N

24
Q

Which AAs contain amides?

A

Asparagine, Asn, N and Glutamine, Gln, Q

25
Q

What is the most common free AA in the blood?

A

Glutamine, Gln, Q

26
Q

Which AA is involved in a wide range of metabolic rxns?

A

Glutamine, Gln, Q

27
Q

Two cysteine residues can come tg to form what kind of bond? What does this do? How can this bond be broken?

A
  • Two cysteine residues to can come tg to form a disulfide bond and produce cystine
  • These bonds help hold tg the tertiary structure of proteins
  • These bonds can be broken via reduction to break up the protein’s tertiary structure and reform the individual thiol groups of each cysteine residue
28
Q

If the electronegativity difference between S and H is only 0.38, why is cysteine still considered a polar amino acid?

A

Bc it can still participate in H-bonding, although rather weakly

29
Q

What is a pirate’s favorite amino acid?

A

Arginine, Arg, R

30
Q

Which amino acid contains a guanidium group?

A

Arginine, Arg, R

31
Q

Which amino acid is the most basic? Why?

A

Arginine, Arg, R bc the positive charge is resonance stabilized

32
Q

Which amino acid is involved in the synthesis of several important biomolecules and plays a role in regulating blood pressure?

A

Arginine, Arg, R

33
Q

Which basic amino acid is only meaningfully basic?

A

Histidine, His, H bc ithe deprotonated version of the side chain predominates at physiological pH, making it predominantley uncharged at physiological pH

34
Q

What is the pKa of the side chain of R? What does this allow it to do?

A

The pKa of the side chain is 6.04, which allows it to act as a buffer at pH levels slightly more acidic than the physiological pH

35
Q

Which is the structurally simplest basic amino acid?

A

Lysine, Lys, K

36
Q

Which basic amino acid has a primary amine? What does this allow?

A

Lysine, Lys, K has a fairly reactive primary amine that allows it to serve as a target for methylation and acetylation

37
Q

What are the positively charged/ basic amino acids?

A

R, K, H

38
Q

What are the negatively charged/ basic amino acids?

A

D,E

39
Q

Does the protonated or deprotonated form of aspartic acid predominate at physiological pH?

A

Deprotonated form AKA aspartate

40
Q

Which amino acid is a structural component in proteins and is an important neurotransmitter?

A

Glutamic acid/ glutamate

MCAT (6 decks)

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