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BIOCHEM LEC > MOD2 L3 > Flashcards

MOD2 L3 Flashcards

1
Q

FIBROUS PROTEINS

3

A

COLLAGEN
ELASTIN
KERATIN

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2
Q

GLOBULAR PROTEINS

2

A

MYOGLOBIN
HEMOGLOBIN

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3
Q
  • Triple helix
  • Has 3.3 residues per turn and a rise per residue nearly twice that of an α-helix
  • Every 3rd amino acid residue is a glycine residue
  • Gly-Pro-X or Gly-Hyp-X
A

COLLAGEN

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4
Q

COLLAGEN

Every 3rd amino acid residue is a

A

GLYCINE RESIDUE

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5
Q

sequence of collagen structure

A

Gly-Pro-X

x could be any rare amino acid (could be hydroxyproline or hydroxylysine)

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6
Q

COLLAGEN STRUCTURE

what do we need in order for us to achieve the hydroxylated form of proline & lysine

A

ASCORBIC ACID IN THE FORM OF ASCORBATE

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7
Q

saan nakukuha ang ascorbate

A

in our diet
Vit C supplement

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8
Q

in the biosynthesis of collagen, we need to have the chain of ____

A

PRE-PROCOLLAGEN ON RIBOSOMES

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9
Q

synonym of protein synthesis

A

TRANSLATION

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10
Q

BIOSYNTHESIS OF COLLAGEN

the ____ directs the pre-procollagen to the RER

A

SIGNAL PROTEIN

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11
Q

BIOSYNTHESIS OF COLLAGEN

removing a certain portion
removal of registration peptides

A

CLEAVAGE

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12
Q

BIOSNTHESIS OF COLLAGEN

cleavage of signal protein forms ____

A

PROCOLLAGEN

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13
Q

process of biosynthesis of collagen

in order

A
  1. chain of pre-procollagen, directed to RER by signal proteins
  2. formation of cleavage of signal protein = forms collagen
  3. hydroxylation of lysine & proline
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14
Q

enzymes in biosynthesis of collagen

A

PEPTIDYL LYSINE HYDROXYLASE
PEPTIDYL PROLINE HYDROXYLASE

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15
Q

addition of OH- group

A

HYDROXYLATION

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16
Q

BIOSYNTHESIS OF COLLAGEN

attachment of sugar to some hydroxylysine residues

A

GLYCOSYLATION

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17
Q

BIOSYNTHESIS OF COLLAGEN (GLYCOSYLATION)

Addition of ____ and ____ to some
hydroxylysine residues.

A

GALACTOSE
GLUCOSE

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18
Q

BIOSYNTHESIS OF COLLAGEN

enzymes required for glycosylation

A

GALACTOSYL TRANSFERASE
GLYCOSYL TRANSFERASE

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19
Q

involves transfer of groups

A

TRANSFERASE

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20
Q

BIOSYNTHESIS OF COLLAGEN

how many α-chains of procollagen are needed to have self association

A

3

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21
Q

BIOSYNTHESIS OF COLLAGEN

what is needed to have stability of procollagen

A

DISULFIDE BONDS

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22
Q

BIOSYNTHESIS OF COLLAGEN

formation of disulfide bonds is called

A

REGISTRATION PEPTIDES

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23
Q

BIOSYNTHESIS OF COLLAGEN

involves the formation of disulfide bonds between parts of the polypeptide chains

A

ASSEMBLY OF THREE α-CHAINS TO FORM PROCOLLAGEN

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24
Q

BIOSYNTHESIS OF COLLAGEN

formation of disulfide bonds between parts of the polypeptide chains known as ____ which occur at both ends of the pre-procollagen.

A

REGISTRATION PEPTIDES

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25
Q

BIOSYNTHESIS OF COLLAGEN

registration peptides are found at the

A

ends of pre-procollagen

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26
Q

BIOSYNTHESIS OF COLLAGEN

The assembly process of 3 α-chains occurs in the

A

GOLGI APPARATUS

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27
Q

BIOSYNTHESIS OF COLLAGEN

Secretion of procollagen molecules by ____ into the extra cellular space

A

EXOCYTOSIS

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28
Q

BIOSYNTHEIS OF COLLAGEN

  • Occurs in the extra cellular space, and is catalyzed by procollagen peptidases.
  • The resulting molecule is called tropocollagen.
A

CLEAVAGE OF REGISTRATION PEPTIDES

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29
Q

BIOSYNTHESIS OF COLLAGEN

the resulting molecule in the cleavage of registration peptides

A

TROPOCOLLAGEN

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30
Q

BIOSYNTHESIS OF COLLAGEN

cleavage of registration peptides occurs in the

A

EXTRACELLULAR SPACE

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31
Q

BIOSYNTHESIS OF COLLAGEN

cleavage of registration peptides is catalyzed by

A

PROCOLLAGEN PEPTIDASES

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32
Q

BIOSYNTHESIS OF COLLAGEN

Self-assembly or polymerization of tropocollagen molecules form

A

COLLAGEN FIBRILS

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33
Q

BIOSYNTHESIS OF COLLAGEN

____ between adjacent tropocollagen molecules stabilizes the fibrils.

A

CROSS-LINKAGE

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34
Q

BIOSYNTHESIS OF COLLAGEN

Self-assembly or polymerization of tropocollagen molecules involves the ____ which has a net oxidative effect and the formation of covalent cross-links.

A

REMOVAL OF AN AMINO GROUP

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35
Q

BIOSYNTHESIS OF COLLAGEN

Self-assembly or polymerization of tropocollagen molecules is catalyzed by

A

LYSINE OXIDASE / CATALASE

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36
Q
  • like a glue
  • holds our joint together
A

COLLAGEN

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37
Q
  • Inheritable defects in collagen molecule;
  • Characterized by stretchy skin and loose joints;
  • Due to defect in genes that encode α- collagen-1, procollagen N-peptidase, or lysyl hydroxylase.
A

EHLERS-DANLOS SYNDROME

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38
Q

a person suffering from this disease has a flexible body structure

A

EHLERS-DANLOS SYNDROME

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39
Q

deficiency in α- collagen-1, procollagen N-peptidase, or lysyl hydroxylase

A

EHLERS-DANLOS SYNDROME

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40
Q
  • severe form of ehlers-danlos syndrome
  • prone in falling; possibility to have bone breakages
A

VASCULAR TYPE

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41
Q
  • Brittle bone syndrome
  • Bones easily bend and fracture
  • stunted growth
  • irregular bone structures
  • permanent disability
A

OSTEOGENESIS IMPERFECTA

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42
Q

osteogenesis imperfecta is also known as

A

brittle bone syndrome

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43
Q
  • Characterized by kinky hair and growth retardation
  • Due to dietary deficiency of copper required by lysyl oxidase, which catalyzes a key step in the formation of the covalent cross-links that strengthen collagen fibers.
  • a genetic disorder caused by a mutation usually primarily in the Y Chromosome (boys) it affects the copper levels and metabolism in the body causing seizures, brain damage, weakened bones and muscles, organ shutdown and failure to thrive.
A

MENKE’S SYNDROME
KINKY HAIR SYNDROME

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44
Q

Menke’s syndrome is otherwise known as

A

KINKY HAIR SYNDROME

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45
Q

common affected by the menke’s syndrome / kinky hair syndrome

A

MALE / BOYS

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46
Q
  • Best known defect in collagen biosynthesis;
  • Deficiency of Vit. C (required by prolyl and lysyl hydroxylases);
  • Bleeding gums, swelling joints, poor wound healing, and ultimately death.
A

SCURVY

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47
Q

required by proline & lysyl hydroxylases

A

VIT C
ASCORBIC ACID

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48
Q
  • Connective tissue protein with rubber-like properties
  • Found in lungs, walls of large blood vessels, and elastic ligaments
  • Can be stretched to several time their normal length, but recoil to their original shape when relaxed.
A

ELASTIN

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49
Q
  • responsible for lung’s elastic property
  • its ability to inflate & deflate
A

ELASTIN

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50
Q
  • Composed primarily of small non polar amino acid residues (e.g. G, A, V).
  • Also rich in proline and lysine, but contains little hydroxyproline and hydroxylysine.
  • Interchain cross-links form desmosine residues.
A

ELASTIN

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51
Q

interchain cross-links of elastin form

A

DESMOSINE RESIDUES

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52
Q

An extensively interconnected, rubbery network that can stretch and bend in any direction when stressed, giving connective tissue elasticity.

A

DESMOSINE CROSS-LINK

53
Q

one of the leading case of non communicable diseases accdng to the DOH

A

EPHYSEMA

54
Q
  • does not have repair mechanism
  • cannot deactivate neutrophil elastases
A

EMPHYSEMA

55
Q

reactive oxygen species (ROS) are also known as

A

FREE RADICALS

56
Q

stimulates pro-inflammatory mediators such as IL-8, LTB, TNF

A

NICOTINE

57
Q

Inhibit neutrophil elastase (protease that degrades elastin of alveolar walls)

A

α-1 antitrypsin

58
Q

Deficiency of α-1 antitrypsin leads to destruction of the alveolar walls of the lungs resulting to

A

EMPHYSEMA

59
Q

treatment for emphysema

A

administration of α-1 AT

60
Q
  • the lungs natural defense against the irritants
  • attach themselves to the foreign material in the sac and consumes it as well as bacteria in the lungs
A

ELASTASE

61
Q

Once the lungs has been cleaned,
____ deactivates elastase.

A

ANTITRYPSIN

62
Q

Without the antitrypsin enzyme, the ____ continues to consume anything in its path, including healthy lung tissue.

A

ELASTASE

63
Q
  • Proteins that forms tough fibers;
  • Found in the hair, nails, and outer epidermal layers of mammals;
  • Constituents of intermediate filaments of cytoskeleton in certain cells.
A

α-KERATIN

64
Q

why hair and nails are insoluble in water

A

non polar R groups are found outside which makes it insoluble in water

65
Q
  • Group of specialized protein that contains heme.
  • Maintain a supply of oxygen essential for oxidative metabolism
    – MYOGLOBIN
    – HEMOGLOBIN
A

GLOBULAR HEMEPROTEINS

66
Q
  • Fe+2- protoporphyrin IX
  • A cyclic tetrapyrrole
  • protein that are produced by amino acids
  • A planar network of conjugate double bonds absorbs visible light and colors heme deep RED.
A

HEME

67
Q

amino acids that are not directly involved in protein synthesis

A

NON PROTEINOGENIC

68
Q
  • A monomeric protein (153 amino acid residues) of the red muscles
  • Used in some tissues, notably muscle,
    – as a storage reserve of O2
    and
    – for intracellular transport of O2
A

MYOGLOBIN (Mb)

69
Q

predominant secondary structure that is visible in the tructure of myoglobin

A

α-helix

70
Q

myo means

A

muscles

71
Q
  • 78% α helical (the other 22% in β turns and short loops, no β sheet at all)
  • 8 α - helices and connections between helices are referred to as “AB”, “CD”, etc.
  • Polar amino acid residues are found at the surface
  • Non polar amino acid residues (L, V, F, & M) are found at the interior except His E7 and HisF8
A

MYOGLOBIN

72
Q

The heme of myoglobin lies in crevices of

A

HELICES E & F

73
Q

SUBUNIT COMPOSITION

Fetal hemoglobin (HbF)

A

α2γ2

74
Q

major hemoglobin in adults

A

HEMOGLOBIN A (HgA)

75
Q

SUBUNIT COMPOSITION

Hemoglobin A

A

α2β2

76
Q

SUBUNIT COMPOSITION

sickle cell hemoglobin (HbS)

A

α2S2

77
Q

SUBUNIT COMPOSITION

minor adult hemoglobin (HbA2)

A

α2δ2

78
Q

have almost identical secondary and tertiary structures

A

Myoglobin and the β polypeptide of hemoglobin

79
Q

composed of two identical
dimers, (αβ)1 and (αβ)2, dimers 1 and 2
respectively

A

Hgb tetramer

80
Q

Dimers are held together by

A

HYDROPHOBIC INTERACTIONS

81
Q

also occur between the members of the dimer

A

IONIC & H-BONDING

82
Q
  • Deoxy form of Hgb
  • Two αβ dimers interact through a network of ionic bonds and hydrogen bonds
A

T FORM OR TAUT (TENSE) FORM

83
Q

Low oxygen-affinity form of hemoglobin

A

T FORM OR TAUT (TENSE) FORM

84
Q
  • Binding of oxygen to Hgb (oxyhemoglobin)
  • Some ionic bonds and H-bonds between the αβ dimers are ruptured thus, the polypeptide chains have more freedom of movement
A

R FORM OR RELAXED FORM

85
Q

High oxygen-affinity form of hemoglobin

A

R FORM OR RELAXED FORM

86
Q

Hemoglobin binding sites per molecule

A

4 O₂

87
Q

____ cooperate in binding oxygen

A

SUBUNITS

88
Q

The oxygen dissociation curve for Hemoglobin is ____ in shape

A

SIGMOIDAL

89
Q

Can bind only one molecule of oxygen (one heme group only)

A

MYOGLOBIN

90
Q

The oxygen dissociation
curve for Myoglobin is a ____ shape

A

HYPERBOLIC

91
Q

reversibly binds a single molecule of oxygen

A

MYOGLOBIN

92
Q
  • It means that the binding of an oxygen molecule at one heme group increases the oxygen affinity of the remaining heme group in the same Hgb molecule
  • This is referred to as heme-heme
    interaction
A

COOPERATIVE BINDING OF OXYGEN

93
Q

cooperative binding of oxygen is also referred to as

A

HEME-HEME INTERACTION

94
Q

cooperative interactions are also called

A

ALLOSTERIC INTERACTIONS

95
Q

allos

A

OTHER

96
Q

STEREOS

A

SPACE

97
Q

a ligand that influences other ligand to bind at a specific site

A

ALLOSTERIC EFFECTOR / MODULATOR

98
Q

occur when binding of one ligand at a specific site is influenced by binding of another ligand

A

ALLOSTERIC INTERACTIONS

99
Q

second site in allosteric interactions

A

ALLOSTERIC SITE

100
Q

the interacting sites all bind the same ligand (e.g., binding of O2 at one site on Hb influences the binding affinity for O2 of another site)

A

HOMOTROPIC INTERACTION/EFFECT

101
Q

the interacting sites bind different ligands

A

HETEROTROPIC INTERACTION/EFFECT

102
Q
  • Positive effect
  • the effector increases the binding affinity for the same kind of ligand at other sites
  • O2 in the hemoglobin system increases the O2 binding affinity of other sites
A

HOMOTROPIC INTERACTION / EFFECT

103
Q

increases the binding affinity for the same kind of ligand at other sites

A

HOMOTROPIC EFFECTOR

104
Q
  • the effector decreases the binding affinity for the primary ligand
  • protons, or CO2, or 2,3-BPG
A

NEGATIVE HETEROTROPIC EFFECTOR / ALLOSTERIC INHIBITOR

105
Q

effector increases the binding affinity for the primary ligand

A

POSITIVE HETEROTROPIC EFFECTOR / ALLOSTERIC ACTIVATOR

106
Q

effect of binding of protons (H+) and CO₂ on O₂ binding affinity of Hb

HbO₂ + H+ ↔ HbH+ + O₂

A

BOHR EFFECT

107
Q

Increase protons or a lower pO₂

A

Deoxyhemoglobin

108
Q

Decrease protons or an increase pO₂

A

Oxyhemoglobin

109
Q

has darker color

oxyhemog or deoxyhemog

A

OXYHEMOGLOBIN

110
Q

CO₂ is a ____ of O₂ binding to Hb

A

NEGATIVE HETEROTROPIC EFFECTOR / ALLOSTERIC INHIBITOR

111
Q

CO binds ____ (but ____) to the Hb iron, forming carbon monoxyhemoglobin, HbCO

A

TIGHTLY, REVERSIBLY

112
Q

CO binding to one or more of the 4 heme sites of Hb shifts to

A

RELAXED CONFORMATION

113
Q

The affinity of Hb for CO is ____ greater than for oxygen

A

220x

114
Q

% of HbCO are fatal

A

60%

115
Q

CO poisoning is treated with ____, which facilitates the dissociation of CO.

A

OXYGEN THERAPY

116
Q

CO %

mild poisoning

A

0,08%

117
Q

CO

moderate posioning

A

up to 0,32%

118
Q

CO

severe poisoning

A

above 1,2%

119
Q
  • Most abundant organic phosphate in the red blood cells
  • Binds strongly to the deoxy form of Hb (T state), but only very weakly to oxy form (R state)
  • Favors/stabilizes the T form, reducing the O2 binding affinity of Hb (shifts binding curve to the right);
  • Increased concentration of 2,3-BPG, reduce affinity of hemoglobin for O2 which increases the efficiency of O2 delivery (enhances RELEASE) to tissues
A

2,3-bisphosphoglycerate (2,3-BPG) or “2,3-diphosphoglycerate” (DPG)

120
Q

Increase concentration of 2,3-BPG is observed in:

A

*Chronic hypoxia
*High altitudes
*Chronic anemia

121
Q
  • The heme iron is ferric than ferrous
  • Oxidation of ferrous to ferric is caused by the side effects of drugs such as sulfonamides, or endogenous substance like hydrogen peroxide
  • Can neither bind nor transport oxygen
A

METHEMOGLOBIN

122
Q

HisF8 has been replaced by tyrosine

A

HEMOGLOBIN M

123
Q

V has replaced Glu6 of the β-subunit

A

HEMOGLOBIN S

124
Q

Dark red coloration of urine following massive crush injury because myoglobin is released from damaged muscle fibers

A

MYOGLOBINURIA

125
Q

Reduction in the number of RBC or of Hb in the blood, or impaired production of erythrocytes (Vit.B12 deficiency)

A

ANEMIA

126
Q

Partial or total absence of one or more α (α-thalassemia) or β (β-thalassemia) chains of hemoglobin

A

THALASSEMIA

127
Q
  • Glucose enters the erythrocytes and glycosylates the α-group of lysine residues and the amino terminal of Hb
  • Reflects the mean blood glucose concentration thus provides valuable information for management of Diabetes Mellitus
A

GLYCATED HEMOGLOBIN (HbA₁c)

128
Q

to know if the patient is resistant to OHAS, the HbA₁c should be around

A

5.7-6.4

BIOCHEM LEC (12 decks)

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