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Basic Biochemistry > 50. Protein structure > Flashcards

50. Protein structure Flashcards

1
Q

set of all proteins expressed by an individual cell at a particular time

A

proteome

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2
Q

aims to identify the entire complement of proteins elaborated by a cell under diverse conditions

A

proteomics

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3
Q

except for this aa, each amino acids has a
•carboxyl group
•amino group
•R group

A

proline

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4
Q

this amino acid is a major inhibitory neurotransmitter in the spinal cord

A

glycine

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5
Q

constitutes as a major fraction of free amino acids in the blood

A

alanine

glycine

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6
Q

Valine
Leucine
Isoleucine
acuumulate in this disease

A

maple syrup urine disease

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7
Q

precursor of tyrosine

A

phenylalanine

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8
Q

precursor of homocysteine

A

methionine

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9
Q

involved in transfer of methyl groups as S-adenosylmethionine (SAM)

A

methionine

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10
Q

imino acid

A

proline

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11
Q

contributes to the fibrous structure of collagen

interrupts alpha helices in globular proteins

A

proline

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12
Q

site of O-linked glycosylation

A

serine
threonine
tyrosine

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13
Q

precursor of dopamine and epinephrine

A

tyrosine

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14
Q

precursor of thyroxine and melanin

A

tyrosine

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15
Q

site for N-linked glycosylation

A

asparagine

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16
Q

major carrier of nitrogen to the liver from peripheral tissues

A

glutamine

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17
Q

carrier of ammonia from skeletal muscle to the liver

A

alanine

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18
Q

precursor of GABA and glutathione

A

glutamate

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19
Q

precursor of histamine

A

histidine

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20
Q

used in diagnosis of folic acid deficiency

A

histidine (FIGIu excretion test)

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21
Q

precursor of creatinine, urea, nitric oxide

A

arginine

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22
Q
  • implicated in neurolathyrism

* progressive and irreversible spastic paralysis of lower extremities

A

Homourginine,

ß-N-Oxalyldiaminopropionic acid

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23
Q
  • neurotoxic amino acid in Cycad seeds

* implicated in ALS-Parkinson dementia complex in natives of Guam

A

ß-methylaminoalanine

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24
Q

amino acid considered nutritionally semi-essential

A

arginine

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25
Q

amino acid that can be synthesized the body

A

cystine

tyrosine

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26
Q

sequencing from N-terminal amino acid

A

•Sanger’s reagent (1-fluoro-2,4-dinitrobenzene)

Edman’s reagent (Phenylisothiocyanate)

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27
Q

sequencing from C-terminal amino acid

A
  • Hydrazine

* carboxypeptidases

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28
Q

secondary structure of proteins is stabilized by

A

hydrogen bonding

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29
Q

most common secondary structurte

A

alpha helix

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30
Q

supersecondary sructures produced by packing side chains from adjacent secondary structural elements close to each other

A

motifs

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31
Q

overall 3-dimensional shape of the protein

A

tertiary strucrure

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32
Q

this protein structure is stabilized by disulfide bonds, hydrophobic interactions, hydrogenm bonds and ionic interactions

A

tertiary structure

33
Q

fundamental functional and 3 dimensional structural units of polypeptide

A

domains

34
Q

number and types of polypeptide units of oligomeric proteins and their spatial arrangement

A

quaternary structure

35
Q

results in unfolding and disorganization of the protein’s secondary and tertiary structures

A

denaturation

36
Q

rescue proteins

required for proper folding of many species of proteins

A

chaperones

37
Q

fatal neurodegenerative diseases characterized by:

•spongiform changes, astrocytic gliomas, neuronal loss

A

prion diseases

38
Q
  • most common and most important degenerative disease of the brain
  • diffuse cerebral atrophy with dementia
  • senile plaques and neurofibrillary bundles
  • aggregates of protein ß-amyloid
A

Alzheimer disease

39
Q

this lipoprotein has been implicated as a potential mediator transformation of soluble alpha helix rich state to beta amyloid that is prone to self-aggregation

A

apolipoprotein E

40
Q

configuration of Hemoglobin with low O2 affinity

A

Taut form (T form)

41
Q

configuration of Hemoglobin with high O2 affinity

300 X

A

R form (relaxed)

42
Q

O2 dissociation curve shows saturation

A

myoglobin

43
Q

O2 dissociation curve shows cooperativity

A

hemoglobin

44
Q

has allosteric effects

a. myoglobin
b. hemoglobin

A

b hemoglobin

45
Q

factors that cause shift to the right of O2 dissociation curve

A
  • ÎÎ CO2
  • ÎÎacidity (dec pH)
  • ÎÎ 2.3 BPG
  • ÎÎ exercise
  • ÎÎ Temp
46
Q

stabilizes the T structure of Hgb by forming additional salt bridges taht must be broken down
prior to conversion to the R state

A

2,3-BPG

47
Q

refers to the observation that increases in the carbon dioxide partial pressure of blood or decreases in blood pH result in a lower affinity of hemoglobin for oxygen.

A

Bohr effect

48
Q

results from the fact that deoxygenated hemoglobin has a higher affinity (~3.5 x) for CO2 than does oxyhemoglobin. Deoxygenated hemoglobin has a higher affinity for CO2 because it is a better proton acceptor than oxygenated hemoglobin. Therefore, when hemoglobin is deoxygenated (i.e., at tissues) there is a right shift of the carbonic acid-bicarbonate buffer equation to produce H+ which in turn increases the amount of CO2 which can be carried by the blood back to the lungs to be exhaled. Then, with oxygenation at the lungs CO2 dissociates more readily from hemoglobin.

A

Haldane effect

49
Q

ζ2 ε2

A

Embryonal hemoglobin (Hb Gower 1)

50
Q

α2 γ2

A

Fetal hemoglobin (HbF)

51
Q

α2 ß2

A

Hemoglobin A (HbA)

52
Q

α2 δ2

A

Hemoglobin A2

53
Q

conception up to first few months

A

Hb Gower 1

54
Q

First few months to after birth

A

HbF

55
Q

8 month onwards

A

HbA

56
Q

cutoff of HbA1C to diagnose DM

A

≥ 6.5%

57
Q

lowering A1C below ____ has been shown to reduce microvascular and neuropathic complications of DM

A

7%

58
Q

for microvascular disease prevention, the A1C goal for nonpregnant adults is

A

<7%

59
Q

when blood glucose enters erythrocytes, it glycosylates

A
  • ε- amino group of lysine residues

* amino terminals of Hgb

60
Q

has 200 x greater affinity for Hgb than O2

A

CO

61
Q

Tx for carboxyhemoglobin

A

100% O2 therapy

62
Q

oxidized form of Hgb (Fe3+) that does not bind O2, but has higher affinity for cyanide

A

methemoglobin

63
Q

s and sx of methemoglobinemia

A

anxiety
headache
dyspnea

O2 sat: 85%

64
Q

chocolate cyanosis

A

methemoglobinemia

65
Q

tx for methemoglobinemia

A

Mild: oral methylene blue
or ascorbic acid
•Acute massive due to ingesiton: IV methylene blue

66
Q

disorder characterized by inherited defect in RBC membrane that renders the erythrocytes speroidal, less deformable and vulnerable to splenic sequestration and detruction

A

hereditary spherocytosis

67
Q

mutations associated with hereditary spherocytosis

A
  • ankyrin (most common)
  • spectrin
  • band 4.1
  • band 3
68
Q

hereditary spherocytosis

manifestations

A
  • anemia
  • splenomegaly
  • jaundice
69
Q

lab test for hereditary spherocytosis

A

osmotic fragility test

70
Q

inheritance of sickle cell disease

A

homozygous recessive disorder

71
Q

results from a point mutation in both genes coding for ß chain that results in a VALINE rather than GLUTAMATE

A

Sickle cell disease

72
Q
  • polymerization and dec solubility of the deoxy form of Hb
  • distortion of the RBC membrane
  • Misshapen, rigid RBC occlude capillaries
A

sickle cell disease

73
Q

manifestations

Sickle cell disease

A

anemia
tissue anoxia
painful crises
protective against malaria

74
Q

tx sickle cell disease

A

hydration
analgesics
antibiotics if with infection , transfusions, hydroxyurea

75
Q

Hgb C disease

Hgb variant that has a single amino acid substitution in ____

A

6th position of the ß-globin chain

•lysine- substituted for glutamate

76
Q

inadequate synthesis of alpha chains

•symptoms appear at birth

A

alpha thalassemia

•alpha chains needed for HbF and HbA

77
Q

leads to anemia, accumulation of Hb Bart (y4) ad Hb H (ß4) and ß chain precipitation

A

alpha thalassema

78
Q

inadequate synthesis of beta chains

A

Beta thalassemia

79
Q
  • symptoms appear after birth

* leads to anemia, accumulation of Hb Barts and alpha chain precipitation

A

Beta thalassemia

Basic Biochemistry (50 decks)

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