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Biochemistry 409 > Amino acids > Flashcards

Amino acids Flashcards

1
Q

Why do we need to eat amino acids

A
  • they are the building blocks of proteins
  • Animals can’t store nitrogen
  • also used as an energy source to generate ATP
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1
Q

What two groups does every amino acid have

A
  • Amino group which are the alpha-amino acids
  • carboxylic acid group attached to the alpha carbon atom
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2
Q

Amphoteric

A

functioning as both an acid and base
- an example are amino acids

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3
Q

zwitterions

A

Molecules that contain both a negative and positive charge

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4
Q

Glycine

A

Also known as Gly or G
- only achiral amino acid
- smallest side chain with only 1H making it’s conformation the most flexible
- Functions as an inhibitory neurotransmitter and is the biosynthesis of purines and hemes
- nonpolar and aliphatic

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5
Q

Alanine

A

known as Ala or A
- rare
- nonpolar and aliphatic

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6
Q

Valine

A

Known as Val or V
- nonpolar and aliphatic

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7
Q

Leucine

A

Known as Leu or L
- In the skeletal muscle, leucine metabolism regulates protein biosynthesis.
-nonpolar and aliphatic

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8
Q

Isoleucine

A

known as Ile or I
- has a second chiral center
-nonpolar and aliphatic

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9
Q

proline

A

known as pro or P
- is unique in that it is a cyclic secondary amino acid.
- has the least conformation flexibility(rigid)
- known as helix breaker
- nonpolar and aliphatic

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10
Q

Methionine

A

known as Met or M
- Methionine has a thioether side chain but still is nonpolar and hydrophobic.
- codes for AUG
- nonpolar and aliphatic

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11
Q

Phenylalanine

A

Also known as Phe or F
- The aromatic ring of phenylalanine is comparable to that of benzene
- It is nonpolar and chemically unreactive

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12
Q

Tyrosine

A

Also known as Tyr or Y
- nonpolar
- biosynthesis of melanin, dopamine, epinephrine and norepinephrinev

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13
Q

How do aromatic rings in amino acids unique and what three amino are they?

A

They are nonpolar so they can absorb light in the ultraviolet region
- phenylalanine @260nm
- tyrosine @280nm
- tryptophan @280nm

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14
Q

Tryptophan

A

Also known as TRP or W
- Tryptophan contains the nonpolar and bulky, aromatic, indole side chain.
- Protonation of the indole nitrogen destroys the aromaticity of the indole ring. The indole side chain is fluorescent making tryptophan fluorescence very useful for studying protein structure.
- Tryptophan is the precursor for the biosynthesis of melatonin and serotonin

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15
Q

Lysine

A

Also known as Lys or K
- Basic
- contains butyl ammonium side chain

16
Q

Histidine

A

Also known as His or H
- Basic
- imidazole functional group. The imidazole ring is aromatic.
- coordinate to metal ions such as zinc, iron, nickel, copper and magnesium

16
Q

Arginine

A

Also known as Arg or R
- Basic
- contains a guanidino group at end of its ide chain

17
Q

Aspartate

A

Also known as Asp or D
- Acidic Amino Acids, Negatively Charged

18
Q

Glutamate

A

Also known as Glu or E
- Acidic Amino Acids,
- function as neurotransmitter and flavor enhancer

19
Q

Asparagine

A

Also known as Asn or N
- Polar, uncharged amino acid

20
Q

Glutamine

A

Also known as Gln or Q
- Polar, uncharged amino acid
- unionizable
- important for maintaining nitrogen balance in cells
- source of ammonia transport excess ammonia from the tissues to the liver

21
Q

Serine

A

Also known as Ser or S
- Polar, uncharged amino acid
- similar to ethanol

22
Q

Threonine

A

Also known as Thr or T
- Polar, uncharged amino acid
- contains a second chiral center

23
Q

Cysteine

A

Also known as Cys or C
- Polar, uncharged amino acid
- Thiol side chain that is unionized
- sulfhydryl of cysteine coordinates to metal ions such as zinc, iron, nickel, copper and magnesium.
- Two cysteines in close proximity can be oxidized to form disulfide bonds.
- most abundant

24
Q

What kind of reactions does cysteines participate in

A

biological redox reactions
-The disulfide bond can join two separate protein chains or crosslink two cysteines within the same chain

25
Q

D pKa

A

3.90

26
Q

E pKa

A

4.10

27
Q

H pKa

A

6

28
Q

K Pka

A

10.5

29
Q

R pKa

A

12.5

30
Q

C pKa

A

8.3

31
Q

Y pKa

A

10.10

Biochemistry 409 (9 decks)

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