Amino acids and Proteins Flashcards

1
Q

What are the essential and nonessential amino acids?

A

1) LLTTVIPMH
2) 4A,3G,CPST

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2
Q

Lysine, Tryptophan, Asparagine, Aspartate, Glutamate, Glutamine letters?

A

K, W, N, D, E Q

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3
Q

Selenocysteine is needed for the functioning of what 2 enzymes?

A

Glutathione peroxidase, Thioredoxin reductase

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4
Q

Proline has a … amine as opposed to the other amino acids that all have a … amine?

A

secondary, primary

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5
Q

All amino acids are chiral except…
Amino acids by convention are in the … form(L or D)

A

Glycine
L

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6
Q

Non-polar A.A. include

A

Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine
(GAVLIM)
Proline is an exception.
VIL= BCAA

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7
Q

Polar neutral A.A. include…

A

Asparagine, Glutamine, Serine, Threonine, Cysteine.
(AGCST)

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8
Q

Function?
1) Hydroxyproline, Hydroxylysine
2) Y-carboxy glutamate
3) Citrulline, Ornithine
4) B-alanine
5) GABA
6) Gaba pentin
7) Penicillamine

A

1) In collagen and myosin
2) In prothrombin
3) Urea cycle
4) intermediate of coA
5) Neurotransmitter from glu
6) epilepsy treatment
7) Wilson disease treatment(chelates copper)

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9
Q

If pH > pI, protein will have a net … charge.
If pH < pI, protein will have a net … charge.

A

-ve, +ve

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10
Q

Pka’s to memorize(0 if pH lower than acid or higher than base)
1) Asp + Glu
2) Cys
3) Tyr
4) His
5) Lys
6) Arg
7) N and C

A

1) around 4
2) 8
3) 10
4) 6 ~ 7
5) 9.5-10
6) 12
7) 9 and 2

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11
Q

Types of bonds involved in:
1) Secondary
2) Tertiary
3) Quaternary

A

1) Peptide
2) R group hydrophobic, salt bridges, and mainly disulfide bonds(covalent)
3) Non-covalent and rare disulfide

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12
Q

Most destructive A.A is…

A

Proline(it has no H-bonds)

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13
Q

Keratin is unique since it

A

Flips between alpha helix and B-sheet(dry hair vs heated)

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14
Q

6 bonds keep iron in the middle of heme…

A

1) 4 N from tetrapyrrole rings
2) Fe-His at F8(proximal His)
3) Fe-His at E7(Distal His = makes it hard for O2 to bind initially and prevents Fe2+ > Fe 3+)

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15
Q

3 factors influence O2 unloading

A

1) decrease in pH(more acid)
2) Increase CO2
3) 2,3-bisphosphoglycerate

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16
Q

Lung > Tissue

A

1) Deoxy hemo in lungs becomes oxy due to high O2 pressure
2) Oxy hemo releases H+ to make carbonic acid
3) Oxy hemo goes to tissues(carbonic acid breakdown) where pH is low and unloading occurs
4) becomes Deoxy again binds CO2 and exhale
5) Repeat

17
Q

… is an endopeptidase that cleaves C terminus of aromatic A.A.

A

Chymotrypsin

18
Q

1) Marfan syndrome
2) Ehlers-Danlos

A

1) Defect in fibrillin
2) Improper triple helix of collagen(Vit C deficiency)

19
Q

Urea and guanidino residues, when added to a protein, destroy…

A

Secondary and tertiary structures

20
Q

1) Sodium deoxycholate
2) SDS

A

1) lipid emulsifier
2) Unfold polypeptide chain

21
Q

What destroys disulfide bonds?

A

Detergents and reducing agents

22
Q

1) HSP 70
2) HSP 60

A

1) Guide for protein final destination
2) Isolation chamber for proper protein folding.
Both use ATP

23
Q

1) Prolyl cis-trans isomerase
2) Protein disulfide isomerase

A

1) trans peptide bond > cis peptide bond
2) reshuffle/modify disulfide bonds(reduced) or create new ones(oxidized)

24
Q

T/F: B-sheets are more toxic than alpha helices.

A

True

25
Q

Patients with HbS maintain a low level of activity so that…

A

Deoxy HbS doesn’t increase in concentration and polymerize