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Biochemistry > Protein Structure > Flashcards

Protein Structure Flashcards

1
Q

___ determined by a protein’s amino acid sequence

A

primary structure

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2
Q

The peptide bond in primary structure attach the ___ group to ___ group

A
  1. Alpha amino group to the alpha carbonyl group of another
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3
Q

What are the characters of peptide bonds?

A
  1. Partial double bond character
  2. Rigid and planar
  3. Generally a trans configuration
  4. Disrupted by hydrolysis
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4
Q

In Sanger’s reagent, which terminal is cleaved first?

A

N-terminal amino acid

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5
Q

The edman’s reagent cleaves what amino acid terminal?

A

N-terminal amino acid

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6
Q

What reagents used for sequencing cleave C-terminal amino acid?

A
  1. Hydrazine

2. Carboxypeptidase

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7
Q

What bonds stabilize secondary structures?

A

hydrogen bonds

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8
Q

___ is a secondary structure that is spiral with side chains extending outwards

A

Alpha helix

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9
Q

What amino acid disrupts the spiral nature of an alpha helix?

A

proline

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10
Q

How many AA per turn does a alpha helix have?

A

3.6 AA per turn

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11
Q

Keratin has what type of secondary structure?

A

alpha helix

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12
Q

___ is when amino acid residues form a zigzag or pleated pattern

A

beta sheet

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13
Q

In beta sheet, the R groups of the amino acid sequence project in what direction?

A

opposite direction

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14
Q

___ are supersecondary structures produced by packing side chains from adjacent secondary structural elements close to each other

A

motifs

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15
Q

Cite examples of motifs

A
  1. Beta-alpha-beta unit
  2. Greek key
  3. Beta meander
  4. beta barrel
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16
Q

___ structure is stabilized by hydrogen bonds, disulfide bonds, hydrophobic interactions, ionic interactions

A

tertiary structure

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17
Q

___ refers to the 3-D shape of the protein

A

tertiary structure

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18
Q

___ are tertiary structure with fundamental functional and 3-D structural units of polypeptide

A

domains

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19
Q

___ refers to the types of polypeptide units of oligomeric proteins and their spatial arrangement

A

Quaternary strucyre

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20
Q

___ are specialized group of proteins required for proper folding of proteins

A

chaperones

they prevent aggregation, can also rescue proteins that are thermodynamicaly trapped

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21
Q

[Prion disease]

PrPsc has what secondary structure

A

beta sheets

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22
Q

[Prion disease]

What is the normal protein that is converted to the pathogenic conformation?

A

PrPc which is an alpha heliz

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23
Q

In alzheimer’s disease, what protein aggregates?

A
  1. protein beta amyloid
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24
Q

What apoliporotein is implicated as a mediator of protein folding in alzheimers disease?

A

apolipoprotein E

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25
Q

Carbon monoxide bound to hemoglobin is called

A

carboxyhemoglobin

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26
Q

Carbon dioxide bound to hemoglobin is called

A

carbaminohemoglobin

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27
Q

[Hemoglobin]

The taut form has __ affinity to oxygen

A

low affinity

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28
Q

[Hemoglobin]

the R form has ___ affinity to oxygen

A

high oxygen affinity

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29
Q

[Hemoglobin]

What for of Fe favors oxygen binding

A

Ferrous = Fe2+

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30
Q

What heme protein is present in heart and skeletal muscle?

A

myoglobin

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31
Q

___ acts as oxygen reservoir

A

myoglobin

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32
Q

myoglobin is considered a what protein structure?

A

tertiary

33
Q

What allosteric factors shift the curve to the right

A
  1. CO2
  2. Acidity (low pH)
  3. 2,3 BPG
  4. Exercise
  5. Temperature
34
Q

Shifting the curve to the right means that the oxygen’s affinity is

A

is decreased

making it harder for hemoglobin to bind to oxygen but makes it easier for hemoglobin to release bound oxygen

35
Q

___ release of oxygen from hemoglobin is enhanced when the pH is lowered or if there is and increase pCO2

A

bohr effect

36
Q

Between oxy and deoxyhemoglobin, which has a greater affinity for protons?

A

deoxy form of hemoglobin has a greater affinity for protons

37
Q

__ describes how oxygen concentration determine hemoglobin affinity for carbon dioxide

A

haldane effect`

38
Q

What is the hemoglobin is the source during the embryonal stage?

A

yolk sac

39
Q

Hemoglobin A appears at what age?

A

8 months onwards

40
Q

The fetal hemoglobin is composed of

A

2 alpha chains

2 gamma chains

41
Q

Hemoglobin chains is composed of __-

A

2 alpha chains

2 delta chains

42
Q

Glycated hemoglobin glycates what amino group?

A

lysine

enters the epsilon amino group of lysine

43
Q

Methemoglobin does not bind to oxygen but has a high affinity for?

A

cyanide

44
Q

[Diagnose]

chocolate cyanosis, saturation is at 85%

anxiety, headache, dyspnea

A

methemoglobin

Tx: oral methylene blue or ascorbic acid

45
Q

What are the mutations of hereditary spherocytosis?

A
  1. Ankyrin
  2. Spectrin
  3. Band 4.1
  4. Band 3
46
Q

Sickle cell disease is an example of what type of mutation?

A

missense point mutation

47
Q

What is the pathology in hemoglobin C disease?

A
  1. Lysine is substituted for glutamate in the 6th position
48
Q

[Classify this alpha thalassemia]

mild anemia, two missing genes,

A

silent carrier

49
Q

[Classify this alpha thalassemia]

moderate to severe anemia,
three missing genese

A

hemoglobin H disease

50
Q

[Classify this alpha thalassemia]

no genes missing, does not have anemia

A

silent carrier

51
Q

[Thalassemia]

Symptoms manifest after birth (around 6 months)

A

beta thalassemia

52
Q

[Thalassemia]

symptoms appear at birth

A

alpha thalassemia

53
Q

What is the most abundant protein in the body?

A

collagen

54
Q

What is the most common form of collagen?

A

type I

55
Q

What amino acid facilitates kinking of collage

A

X: proline

56
Q

What amino acids are found in collagen

A
  1. Proline

2. Glysine

57
Q

What cells in the body produce collagen?

A
  1. Fibroblast
  2. Osteoblast
  3. Chondroblast
58
Q

What monosaccharide is added to hydroxylysine in the formation of collagen?

A
  1. Galactose

2. Glucose

59
Q

[Synthesis of collagen]

The preprocollagen is synthesized in which part of the cell?

A

rough endoplasmic reticulum

60
Q

[Synthesis of collagen]

What step requires hydroxylation?

A

hydroxylation of proline and lysine

the higher the proline, the more rigid the protein

61
Q

[Types of collagen]

Seen in bone

A

Type I

62
Q

[Types of collagen]

seen in cartilage

A

Type II

63
Q

[Types of collagen]

reticulin

A

Type III

64
Q

[Types of collagen]

basement membrane

A

Type IV

65
Q

[Diagnose]

Hyperextensibility of skin, abnormal tissue fragility, increased joint mobility

A

ehlers-danlos

66
Q

[Diagnose: type of Ehlers Danlos]

defect in type I and type V

more severe skin abnormalities, less severe joint changes

A

classical

67
Q

[Diagnose: type of Ehlers Danlos]

joint hypermobility, osteoarthritis, severe pain

most common

A

hypermobility

Type III

68
Q

[Diagnose: type of Ehlers Danlos]

fragile blood vessels, small stature, transluscent skin,

increased intracranial aneurysms

A

Vascular

69
Q

[Diagnose]

mutatin in collagen genes resulting to bones that can easily bend and fracture

A

osteogenesis imperfecta

70
Q

[Diagnose]

blue sclerae, hearing loss, dental imperfections

A

osteogenesis imperfecta

71
Q

[Diagnose]

hematuria, ocular presentation, hearing loss, type IV collagen mutation

A

alport syndrome

72
Q

[Diagnose]

skin breaks and blisters after a minor trauma; mutation is type VII collagen

A

epidermolysis bullosa

73
Q

[Diagnose]

kinky hair, growth retardation, decreased copper (needed by lysyl oxidase)

A

menkes disease

74
Q

What connective tissue is responsible for the rubber-like properties of a tissue (extensibility, elastic recoil)

A

elastin

contains more proline and lysine

75
Q

[Diagnose]

mutation in fibrillin 1 hene

A

marfan

76
Q

[Diagnose]

taller, thinner
doliochostenomeila, arachnodactyly, upward dislocation of lens

A

marfan syndrome

77
Q

what enzyme inhibits proteolytic enzyme from hydrolyzing and destroying proteins

A

alpha 1 antitrypsin

78
Q

A decrease in alpha 1 antitrypsin in the lungs can lead to an increase in what proteolytic enzyme?

A

elastase

which can destroy proteolytic enzyme

Biochemistry (28 decks)

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