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Biochemistry > Amino Acids > Flashcards

Amino Acids Flashcards

1
Q

How many natural occurring standards amino acids ?

A

20

  • alpha- amino acids
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2
Q

pKa Carboxy group

A

~ 2

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3
Q

pKa Amino group

A

~9.5

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4
Q

Charge of amino (NH3) groups at physiological conditions (pH=7.4)

A

POSITIVE

  • The pH is lower than pKa for the amino group. Therefore, most of the amino- groups are protonated.
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5
Q

Charge of carboxylic (COOH) groups at physiological conditions

A

NEGATIVE

  • The pH is higher than the pKa for the carboxylic group. Therefore, most of the carboxylic groups are deprotonated
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6
Q

At physiological conditions (pH=7.4), all amino acids are in which form? (there are exceptions)

A

ionized form

  • zwitterionic:
    • positive charge- amino
    • negative charge- carboxylic
    • Net charge= 0
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7
Q

Isoelectric Point (pI)

A
  • amino acid is on its zwitterionic form
  • pH at which an amino and a carboxylic group are both charged. And, the sum of their charges is equal to 0.
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8
Q

Glycine

A

bends and turns

OR

tightly packed chains of fibrous proteins like collagen

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9
Q

Branched chain amino acids

A

VIL

  • Val
  • Ile
  • Leu
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10
Q

Sulfur containing amino acids

A
  • Methionine
  • Cys (disulfide bonds- oxidative condensation)
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11
Q

Proline

A
  • Imino acid: amino group is enclosed in a ring
  • NOT found in alpha- helix, is a helix breaker
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12
Q

Aromatic Amino Acids (aromatic rings)

A
  • Trp
  • Phe
  • Tyr
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13
Q

Basic amino acids, positively charged

A
  • Arg
  • Lys
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14
Q

Histidine

A
  • imidazole ring
  • weak basic
  • physiological buffer
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15
Q

Acidic amino acids, negatively charged

A
  • Asp
  • Glu
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16
Q

Hydroxyl (OH) containing

A
  • Ser
  • Thr
  • Tyr
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17
Q

Non- polar, uncharged, aliphatic amino acids

A
  • Gly
  • Ala
  • Pro
  • Val
  • Leu
  • Ile
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18
Q

Polar, uncharged amino acids/ Hydrophillic

A

Asn

Gln

Ser

Thr

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19
Q

Hydrophillic

A

Acidic and basic AAs and polar uncharged.

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20
Q

Titration curves

A

Illustrate changes in amino acid structure that occur as the pH of the solution is changed from <1 to 14 (pH) with a strong base

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21
Q

predominant basic amino acids (pKa> 10)

A

Arg Lys

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22
Q

Semi- essential amino acids

A

Required ONLY during positive nitrogen balance conditions

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23
Q

Define Essential Amino Acids

A

cells cannot synthesize them, they have to be ingested

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24
Q

Define nitrogen balance

A

is the (normal) condition where the amount of nitrogen incorporated into body each day exactly equal the amount excreted

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25
Q

Define Positive nitrogen balance conditions

A

When the amount of nitrogen incorporated into body each day exceeds the amount excreted

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26
Q

Conditions of negative nitrogen balance need Essential AAs

A
  • protein malnutrition
  • dietary deficiency of at least 1 essential AA
  • Starvation
  • uncontrolled diabetes
  • Infection
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27
Q

What are the Essential amino- acids?

A

8 (TV TILL PM) Trp (W) Val (V) Thr (T) Ile (I) Leu (L) Lys (K) Phe (F) Met (M)

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28
Q

What are the non- essential amino acid

A

8 Asp (D) Glu (E) Gly (G) Asn (N) Gln (Q) Ala (A) Ser (S) Pro (P)

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29
Q

normal pH blood?

A

7.4

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30
Q

amino at 7.4

A

protonated

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31
Q

carboxy at 7.4

A

deprotonated

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32
Q

His

A

+/- pKa buffer

33
Q

pH equation

A

pH= pKa when [HA]=[A-]

34
Q

Sickle cell anemia

A

Glutamate (polar) is substituted by Valine (hydrophobic) at B- subunit

35
Q

Blood protein that works for transporting molecules

A

Albumin

36
Q

How the Separation of proteins is performed?

A

In an Electric field proteins are negative and migrate toward the positive electrode

37
Q

Rate of migration of separation of proteins is determined by?

A

net negative charge more negative = faster

38
Q

pH stomach

A

1.5 HCl

39
Q

Aspirin pH

A

3.5 (weak acid)

40
Q

Aspirin at the stomach is ?

A

largely protonated uncharged therefore it can cross the membrane and be absorbed

41
Q

Diabetes- ketoacidosis

A

inadequate insulin increased breakdown of fatty acids in the liver

42
Q

Diabetic ketoacidosis

A

ketone bodies; acetoacetic acid beta- hydroxybutyric acid

43
Q

ketone bodies

A

produce anions and H+ ions lower blood/ cell pH metabolic acidosis

44
Q

metabolic acidosis

A

physiological effects of lower blood pH, including renal disease

45
Q

Q: Is the substitution of a glutamate for valine in sickle cell hemoglobin a conservative replacement?

A

No, is a replacement of an acidic amino acid which is hydrophilic for a non- charged aliphatic AA

46
Q

Q: Is the substitution of an Aspartate for a Glutamate a conservative replacement?

A

Yes, the AA that is being replaced, is being replaced by one AA that is similar in structure, acidic and charged in blood pH

47
Q

Practice: proteolytic digestive enzyme chymotrypsin cleaves the peptide bonds formed by the carboxyl groups of large, bulky uncharged amino acids. Which amino acids fall into this category?

A

Phenylalanine (Phe) Tyrosine (Tyr) Tryptophan (Trp)

48
Q

Practice:

  • Does the following peptide is able to form an internal disulfide bond?
    • Gly- Cys- Glu- Ser- Asp-Arg- Cys
A

Yes, it has 2 Cysteine AAs

49
Q

Practice: A drug sometimes injected as a local anesthetic has only one ionizable group, an amino group with a pKa of 8.6. it is otherwise hydrophobic, and enters cells through free diffusion. The ionized form of the drug acts by binding to the intracellular domain of an ion channel. A localized infection decreased the pH around the site of injection from 7.4 to 6.8. The binding site of the channel for the drug is most likely to contain which one of the following amino acid side chains?

A

Drug: 1 ionizable group (an amino with 8.6) Localized infection: pH= 6.8 Binds to an intracellular domain of an ion channel. Drug: binding site of the channel for the drug: Negatively charged aspartyl or glutamyl residue(s)

50
Q

Where do you find hydrophilic amino acids in a transmembrane and globular protein?

A

outwards

51
Q

Where do you find hydrophobic amino acids in a transmembrane and globular protein?

A

hidden from water, inside

52
Q

Why Methionine is hydrophobic although contains sulfur?

A

it doesnt contain an H and is steric hindrant

53
Q

Basic amino acids can form ionic bonds with ?

A

Acidic amino acids (Arg, Lys, His)

54
Q

Why Pro is called the helix breaker?

A

because on its presence, it changes the direction of the helix, produces a kink

55
Q

Hydrophillic amino acids

A

amide groups and OH groups can form Hydrogen bonds and are located at the surface of globular proteins

56
Q

Hydrophobic amino acids

A

PIMP GAL TV

57
Q

Derived amino acids are product of the

A

Cystine (union of two Cys) Hydroxy- proline hydroxy- lysine

58
Q

Most common post- translational modifications (enzyme required)

A

Hydroxylation Phosphorylation Glycosylation Acetylation

59
Q

Hydroxylation

A

Pro Lys impart strength to collagen

60
Q

Phosphorylation- Metabolic regulation, cell regulation

A

Ser Tyr Thr

61
Q

Glycosylation: O- linked

A

Ser and Thr

62
Q

Acetylation

A

important in gene expression, acetylation of histones at Lys residues

63
Q

pH > pKa

A

Deprotonated form for the species (negative form)

64
Q

pH= pKa

A

Zwitterionic form/ Isoelectric point

65
Q

pH < pKa

A

Protonated form predominating for the species

66
Q

semi essential amino acids are required during?

A

periods of positive nitrogen balance

67
Q

Normal Pattern of Serum Electrophoresis

A
68
Q

Normal Ectrophoretic Racing

A
69
Q

Normal Electrophoretic patterns

A
70
Q

Electrophoretic patterns will change in certain diseases/ conditions

A
71
Q

Immediate Response Electrophoretic Pattern

A
72
Q

Delayed Response electrophoretic pattern

A
73
Q

Hypogammaglobulinemia Electrophoretic Pattern

A
74
Q

Hepatic cirrhosis electrophoretic pattern

Hepatic cirrhosis = polyclonal gammopathy*

A
75
Q

Paraprotein electrophoretic pattern

A
76
Q

Nephrotic Syndrome Electrophoretic Pattern

A
77
Q

Protein losing enteropathy electrophoretic pattern

A
78
Q
A
79
Q

Conditions of Positive Nitrogen Balance

A
  • pregnancy
  • growth
  • recovery from surgery or injury
  • recovery from negative nitrogen balance

Biochemistry (7 decks)

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