Amino Acids Flashcards

1
Q

How many amino acids incorporated into proteins?

A

20

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2
Q

All amino acids exist in the L-form, except for what?

A

Glycine

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3
Q

Why glycine does not exist in the L-form?

A

Because glycine does not contain a “CHIRAL BOND”

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4
Q

What is chiral bond?

A

It is different compounds at each binding site

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5
Q

All amino acids are amphoteric. What is amphoteric?

A

It means all amino acids can act as an whether acid or base. It depends on pH level.

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6
Q

List essential amino acids.

A

Phenylalanine, Valine, Tryptophan
Threonine, Isoleucine, Methionine
Histidine, Arginine, Leucine, Lysine

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7
Q

What are purely ketogenic amino acids?

A

Leucine and Lysine

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8
Q

What is purely ketogenic?

A

. Unable to become glucose
. Glucogenic amino acid
. Ketone body, which used in heart, brain, muscle (as energy)

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9
Q

Lysine precursor to _____?

A

Carnitine

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10
Q

What is carnitine?

A

It takes fatty acids into mitochondria for B-oxidation (burn FAT)

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11
Q

What are the aromatic amino acids?

A

. Phenylalanine, tyrosine, tryptophan.

. It does have benzene ring

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12
Q

What are sulfur-containing amino acids?

A

. Cysteine, methionine, and cystine

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13
Q

What does make cystine?

A

2 cysteine make a cystine.

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14
Q

What are the Branched-chain amino acids?

A

Isoleucine, leucine, and valine

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15
Q

What is Maple syrup urine disease?

A

Cannot break down branched chain amino acids.

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16
Q

What are acidic amino acids?

A

Aspartic acid (aspartate) and glutamic acid (glutamate)

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17
Q

What dose aspartame contain? And if it does exceed, what happened?

A

Contains aspartic acids. Too much can cause neurotoxic.

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18
Q

What are the basic amino acids?

A

Histidine, lysine, and arginine.

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19
Q

When does basic amino acids have the greatest postivie net charge?

A

At normal pH of blood.

20
Q

Phenylalanine convert to what?

A

Tyrosine

21
Q

If there is deficiency of phenylalanine hydroxylase, what happened?

A

PKU (phenylketonuria)

22
Q

Tyrosine -> _-dopa -> ________ -> ________ -> _________

A

L-dopa, dopamine, norepinephrine, epinephrine

23
Q

L-dopa can be convert to melanin as well. What happened if L-dopa failed to convert to melanin?

A

Albinism

24
Q

Tyrosine can convert to T_ and T_.

A

T3 and T4

25
Q

Histidine can convert to what?

A

Histamine

26
Q

Tryptophan can convert to _______ -> _______ ?

A

Serotonin, melatonin(sleeping)

27
Q

Tryptophan can convert to _____ -> _______ ? (Which is relate to vitamin B3 and energy production.)

A

Niacin, nicotinamide

28
Q

For every 10 kg body weight need how much protein?

A

8g protein

29
Q

What is the meaning of isoelectric point?

A

pH when an amino acid has no net electrical charge (neutral)

30
Q

What is Zwitter ion?

A

An AA at its isoelectic point

31
Q

What is compound of glutathione?

A

Tripeptide of glycine, glutamate, and cysteine

32
Q

What is selenium (Se)?

A

It is mineral for enzyme Glutathione peroxidase

33
Q

What is insulin?

A

. 2 poly peptide chains linked by disulfide bond.

. Is not part of the animal cell membrane, but help glucose enter the cell

34
Q

Examples of polypeptide hormones

A

Insulin, glucagon

35
Q

Examples of catecholamine

A

Epinephrine, norepinephrine

36
Q

Example of steroid

A

Testosterone, cortisol, estrogen, progesterone

37
Q

The characteristic bond of all proteins is what?

A

Peptide bond

38
Q

The peptide bond is a type of ____ bond that is specific for proteins.

A

Amide

39
Q

Peptide bond aka _____ bond aka ______ bond

A

C-N bond and Carboxyl-amino bond

40
Q

Protein structure:

1’ (primary)

A

Linear sequence of amino acids.

“Ticker tape” - straight line

41
Q

Protein structure:

2’ (secondary)

A

. Alpha helices and beta pleated sheet.
. Weak bonds
. DNA strands together is example

42
Q

Alpha helices and beta pleated sheet are held together by what?

A

Hydrogen bonds between atoms of the polypeptide backbone.

43
Q

Protein structure:

3’ (tertiary)

A

Folding of a single polypeptide chain in solution.

44
Q

What is the classic example of a globular protein with tertiary structure?

A

Myoglobin (disulfide bond)

45
Q

Protein structure:

4’ (quaternary)

A

Association of two or more poly peptide chains to make a functional protein.

46
Q

What is the classic example of 4’ structure?

A

Hemoglobin (alpha2beta2) (hydrogen & disulfide bonds)

47
Q

Hemoglobin also allosteric compound. So what does it mean?

A

Oxygen will change conformational shape.