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Pearls > Biochem Protein Metabolism > Flashcards

Biochem Protein Metabolism Flashcards

0
Q

Name that amino acid

Basic amino acids

A

“HAL”

Histidine
Arginine
Lysine

  • weak base
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1
Q

Name that amino acid

Acidic amino acids

A

Aspartate and Glutamate

  • negative at physiologic pH
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2
Q

Name that amino acid

Smallest side chain

A

Glycine

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3
Q

Name that amino acid

Largest side chain

A

tWiptophan

  • double v = double ring
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4
Q

Name that amino acid

Causes kinks in collagen

A

Proline

  • IMIno acid, not an amino acid!!!
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5
Q

Name that amino acid

Plays a role in oxygen binding to hemoglobin and myoglobin

A

Histidine

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6
Q

Name that amino acid

Transfer of methyl groups as SAM

A

Methionine

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7
Q

Name that amino acid

Diagnosis of folic acid deficiency

A

Histidine

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8
Q

Nutrially essential amino acid

A

PVT TIM HALL

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9
Q

Name that amino acid

HemoGLobin synthesis

A

GLycine

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10
Q

Name that amino acid

Precursor of Niacin

A

TWiptophan (B6)

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11
Q

Name that amino acid

Precursor of nitric acid

A

Arginine

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12
Q

Name that amino acid

Precursor of melanin

A

Tyrosine

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13
Q

Name that amino acid

Precursor of catecholamines

A

Tyrosine

Catecholamines: Dopamine, Epinephrine, Norepinephrine

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14
Q

Name that amino acid

Precursor of melatonin

A

TWiptophan

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15
Q

Name that amino acid

Precursor of GABA

A

Glutamate

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16
Q

Name that amino acid

Precursor of histamine

A

Histidine

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17
Q

Name that amino acid

Precursor of thyroid hormones

A

Tyrosine

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18
Q

Name that amino acid

Precursor of tyrosine

A

Phenylalanine

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19
Q

Name that amino acid

Precursor of glutathione

A

Glutamate

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20
Q

Name that amino acid

Precursor of homocysteine

A

Methionine –> Homocysteine –> Cystine

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21
Q

Level of protein structure?

Beta pleated sheet

A

Secondary structure

  • forms helix
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22
Q

Level of protein structure?

Sequence of amino acids

A

Primary structure

  • peptide bond
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23
Q

Level of protein structure?

Determine whether protein is globular or fibrous

A

Tertiary structure

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24
Q

Level of protein structure?

More than one polypeptide

A

Quarternary structure

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25
Q

Level of protein structure?

Edman’s reagent

A

Primary structure

-Used for sequencing

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26
Q

Level of protein structure?

Domains

A

Tertiary structure

  • determines FUNCTION!!!
  • domains determine fundamental functional and three dimensional structure, formed by combination of motifs
  • held together by disulfide/hydrophobic/hydrogen/ionic bonds
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27
Q

Level of protein structure?

Domain

A

Secondary structure sin function

  • secondary structure : hydrogen bond
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28
Q

Level of protein structure?

Hemoglobin

A

Quarternary structure

  • non covalent bonds
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29
Q

Hemoglobin or Myoglobin?

Contains heme

A

Both

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30
Q

Hemoglobin or Myoglobin?

Fibrous protein

A

Neither

31
Q

Hemoglobin or Myoglobin?

Only exhibits tertiary structure

A

Myoglobin

32
Q

Hemoglobin or Myoglobin?

Found in heart and skeletal muscle

A

Myoglobin

33
Q

Hemoglobin or Myoglobin?

Binds four molecules of oxygen at a time

A

Hemoglobin

34
Q

Hemoglobin or Myoglobin?

Binding of oxygen is affected by changes in pH and CO2 concentration

A

Hemoglobin

35
Q

Hemoglobin or Myoglobin?

Reservoir of oxygen

A

Myoglobin

36
Q

Hemoglobin or Myoglobin?

Exists in taut and relaxed form

A

Hemoglobin

37
Q

Hemoglobin or Myoglobin?

Sigmoidal oxygen dissociation curve

A

Hemoglobin

Note: myogbin with Hyperbolic curve ( hordes oxygen)

38
Q

Identify the hemoglobin

Most abundant form in adults

A

Hemoglobin A

  • 2 alpha 2 beta
39
Q

Identify the hemoglobin

Hemoglobin bound to 4 oxygen molecules

A

R form (Relaxed)

40
Q

Identify the hemoglobin

Hemoglobin without any oxygen molecule bound to it

A

Taut form

“Crossed arms not carrying any oxygen”

41
Q

Identify the hemoglobin

Non-enzymatic addition of glucose to hemoglobin, used to determine level of control of diabetes mellitus

A

HBA1C

Normal: 6.5
Target in DM: < 7%

42
Q

Identify the hemoglobin

Oxidation of the heme component of hemoglobin to Fe3+, which cannot bind oxygen

A

Methemoglobin

  • O2 saturation 85%
  • Chocolate colored blood
43
Q

Identify the hemoglobin

Carbon monoxide binds tightly but reversibly to the hemoglobin iron

A

Carboxyhemoglobin

  • cherry pink
  • O2 saturation : 100%
44
Q

Identify the hemoglobin

Carbon dioxide bound to hemoglobin for transport in the blood

A

Carbaminohemoglobin

45
Q

Identify the hemoglobin

Tetramer consisting of 2 alpha chains and 2 gamma chains

A

Fatal hemoglobin

46
Q

Identify the hemoglobin

Gamma tetramer in the newborn

A

Hemoglobin Barts

47
Q

Collagen types

Most common?

A

Type 1

  • bone, late wound repair/kelloid
48
Q

Collagen types

Basement membrane

A

Type IV

49
Q

Collagen types

Granulation tissues

A

Type 3

  • threticulate, early repair
50
Q

Collagen types

Ridiculing, Blood vessels

A

Type III

51
Q

Collagen types

Nucleus pulposus, vitreous body

A

Type II

  • also carTWOlage
  • pliant, flexible
52
Q

Collagen types

Tendon, fascia

A

Type 1

  • bONE
53
Q

Positive or Negative nitrogen balance

Pregnancy

A

Positive nitrogen balance

54
Q

Positive or Negative nitrogen balance

Malignancy

A

Negative nitrogen balance

55
Q

Give 3 compound in which organisms excrete nitrogen

A

Ammonia
Uric acid
Urea

56
Q

Through this enzyme, amino acids transfer their amino acids to glutamate

A

Aminotransferases

  • addition of ammonia
57
Q

Through this enzyme, glutamate is oxidatively deaminated to liberate free ammonia

A

Glutamate dehydrogenase

  • glutamate is basurero. G for garbage man:)
58
Q

Enzyme used: glutamine is deaminated to glutamate in kidneys and intestines

A

Glutaminase

59
Q

Enzyme used: glutamine is synthesized from glutamate and ammonia

A

Glutamate synthase

60
Q

Which 3 compounds are the immediate donors of the atoms of urea?

A

1 carbon dioxide

From glutamate:
2 Free ammonia
3 Aspartate

61
Q

Transamination of alanine

A

Pyruvate

62
Q

Transamination of glutamate

A

Alpha ketoglutarate

63
Q

Transamination of aspartate

A

Oxaloacetate

64
Q

Amino acids that are purely ketogenic

A

Lysine
Leucine

P * both Ketogenic and Glucogenic
V
T

T * both Ketogenic and Glucogenic
I * both Ketogenic and Glucogenic
M

H
A
L Ketogenic
L Ketogenic

65
Q

Both Glucogenic and Ketogenic

A

FYI doble V

F phenylalanine
Y tyrosine
I isoleucine
Doble V (W) Tryptophan

66
Q

Identify the glycosaminoglycan

Important coagulant

A

Heparin

67
Q

Identify the glycosaminoglycan

Attracts water in to the ECM

A

Hyalorunic acid

68
Q

Identify the glycosaminoglycan

Determines charge selectiveness of renal glomerulus

A

Heparin sulfate

69
Q

Identify the glycosaminoglycan

Located at sites of calcification of endochondral bone

A

Chondroitin sulfate

70
Q

Identify the glycoproteins

Lubricant and protective agent

A

Mucin

71
Q

Identify the glycoproteins

Transport molecules

A

Tansferrin

Ceruloplasmin

72
Q

Identify the glycoproteins

Immunologic molecules

A

Immunoglobulins

73
Q

Identify the glycoproteins

Oligosaccharide in blood type A

A

N acetyl galactosamine

74
Q

Identify the glycoproteins

Oligosaccharide in blood type B

A

Galactose

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