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Biochemistry 1 > Globular & Fibrous Proteins > Flashcards

Globular & Fibrous Proteins Flashcards

1
Q

Globular proteins has peptide chains folded into _____ or _____ _____

A

Spherical or globular shapes

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2
Q

Hydrophobic side chains are in the ____

A

Interior

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3
Q

Polar side chains are on the

A

Exterior

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4
Q

5 example of globular proteins

A

Hemoglobin, immunoglobulin, myoglobin, insulin, transferrin

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5
Q

Two proteins, myoglobin and hemoglobin are ___ proteins

A

Heme

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6
Q

Proteins that maintain a supply of oxygen essential for oxidative phosphorylation

A

Heme proteins

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7
Q

Heme Proteins maintain a supply of oxygen essential for?

A

oxidative phosphorylation

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8
Q

A cyclic tetrapyrrole linked by methylene bridges

A

Heme

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9
Q

Resides at the center of the planar ring

A

Ferrous ion

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10
Q

The oxidation of ferrous to ____ ion destroys biological activity of these proteins thus giving the blood a ___ color.

A

Ferric , red

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11
Q

A MONOMERIC protein

A

Myoglobin

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12
Q

Myo in myoglobin means

A

Muscles

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13
Q

Tetrameric protein

A

Hemoglobin

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14
Q

Myoglobin is found in ____ that serves as reservoir in times of oxygen deprivation

A

Red muscles

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15
Q

Myoglobin is rich in?

A

a-helices (75%)

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16
Q

The a-helices contains two special histidine residue.

A

His E7 and His F8

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17
Q

His E7 (distal histidine) and His F8 (proximal
histidine). These two residues lie close to the
____ and assist in ____

A

heme iron, oxygen binding.

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18
Q

A tetrameric protein found in ___
which transport oxygen to the ____ and
returns carbon dioxide and protons to the
lungs

A

erythrocytes, tissues

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19
Q

A tetrameric protein found in erythrocytes
which transport ____ to the tissues and
returns _____ to the
lungs

A

oxygen, carbon dioxide and protons

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20
Q

Hemoglobin is a multi-subunit protein represented by
,

A

𝛼2𝛽2

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21
Q

the ____ of hemoglobin closely resemble
the structure of myoglobin.

A

𝛽 subunits

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22
Q

present in
hemoglobin provide additional mechanisms of
control.

A

Allosteric sites

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23
Q

(for regulation; molecules
can bind here

A

Allosteric sites

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24
Q

an oxygen molecule
binds more readily to hemoglobin if other
oxygen molecules are already bound

A

Cooperative binding

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25
Q

Hemoglobin can bind up to

A

4 oxygen
molecules, one per heme.

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26
Q

The subunits of hemoglobin Γ§an exist in two states

A

Relaxed and Taut State

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27
Q

more open; oxygen has higher affinity for
this state;

A

Relaxed

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28
Q

tighter structure; oxygen has lower affinity for
this state;

A

Taut

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29
Q

default state when oxygen concentration is high

A

Relaxed

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30
Q

default state when oxygen is absent

A

Taut

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31
Q

The ability of hemoglobin to
reversibly bind oxygen is affected
by the

A

𝑝𝑂2

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32
Q

Binding of 𝑂2, in hemoglobin
drives the release of .

A

𝐢𝑂2

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33
Q

Hemoglobin (Hb) binds _____ with increasing affinity.

A

Oxygen

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34
Q

Binding of 𝑂2, in hemoglobin
drives the release of 𝐢𝑂2. This
is depended upon the
cooperative interactions
between the hemes of the

A

hemoglobin tetramer.

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35
Q

Effect of
______
Stabilizes the Taut state and promotes
release of 𝑂2.

A

2,3-bisphosphoglycerate

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36
Q

Effect of
2,3-bisphosphoglycerate
Stabilizes the ___ and promotes
release of ___.

A

Taut state, 𝑂2

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37
Q

The role of 2,3-biphosphoglycerate is especially
significant for ____ where
pressure of 𝑂2 is low.

A

high altitudes

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38
Q

Imagine your
climbing to the top of the mountain, once
your body feels ____ __ ____ due
to the increase of altitude, the ____
tries to release the stored oxygen, to
supply it to the body.

A

depletion of oxygen, 2,3-BPG

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39
Q

This is similar to
____ who wore ____
behind them when diving in a deep
ocean.

A

scuba divers, oxygen tanks

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40
Q

Have traditionally been defines as a family of genetic
disorders caused by production of a structurally
abnormal hemoglobin molecule.

A

HEMOGLOBINOPATHIES

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41
Q

Common Hemoglobinopathies:

A
  1. Sickle Cell Anemia (Hemoglobin S disease)
  2. Hemoglobin C disease
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42
Q

Glu amino acid is mutated to a Val

A

Sickle Cell Anemia (Hemoglobin S disease)

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43
Q

Glu amino acid is mutated to Lysine

A

Hemoglobin C disease

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44
Q

has an elongated shape

A

Fibrous protein

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45
Q

Fibrous protein tends to have ____, ___, ____, structures

A

simple, regular, and
linear

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46
Q

tend to aggregate together to form
macromolecular structures

A

Fibrous protein

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47
Q

Examples of fibrous protein

A

Keratin and collagen

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48
Q

Is a component of bone and connective tissue

A

Collagen

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49
Q

Collagen is the the most
abundant protein in ____.

A

vertebrates

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50
Q

Collagens structure is organized in
______ ____ of great strength

A

water-insoluble fibers

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51
Q

A _____ consists of three polypeptide chains
wrapped around each other in a ropelike twist or triple
helix.

A

collagen fiber

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52
Q

These three strands or polypeptide chains are held together by ___
bonds

A

hydrogen

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53
Q

These hydrogen bonds involves

A

hydroxyproline and hydroxylysine
residues

54
Q

Collagen is both intramolecularly and intermolecularly
linked by ____.

A

covalent bonds

55
Q

___ increases with
age.

A

Cross-linking

56
Q

amino acids of
collagen structure are arranged in a repetitious tripeptide sequence,
Gly – X – Y, in which X can be any amino acids but is
frequently a ____ and Y is frequently a ___ or ____

A

Proline, hydroxyproline
or hydroxylysine.

57
Q

Gly – X – Y – Gly – X – Y – Gly – X – Y –

Supply x and Y

A

Gly – Pro – Hyp – Gly – Pro – Hyl – Gly – Pro – Hyp

58
Q

Normal collagens are ___ ___ molecules, having
half-lives as long as several years.

A

highly stable

59
Q

Collagen has an _____, ___-___ structure that places many of its amino acid
side chains on the surface of the triple-helical molecule.

A

elongated,
triple-helical

60
Q

The structure of collagen as triple helical: Resulted to bonding of the exposed ____ of
neighboring collagen monomers, thus the aggregations
into a very long fibers.

A

R-groups

61
Q

In short, amount of
collagen will decrease
as we grow. Thus
wrinkles and fine lines
appear in our face, a
proof that skin collagen is ____

A

depleting.

62
Q

COLLAGEN DISEASES: ___

A

Collagenopathies

63
Q

This disorder is a
heterogeneous group of generalized connective tissue
disorders that result from inheritable defects in the
metabolism of fibrillary collagen molecules.

A

Ehlers-Danlos syndrome (EDS)

64
Q

This disease is a heterogeneous
group of inherited disorders distinguished by bones that
easily bend and fracture.

A

Osteogenesis imperfecta (OI)

65
Q

Retarded wound healing and a
rotated and twisted spine leading to a β€œ____”
appearance are common features of this disease.

A

humped-back

66
Q

The ____ of hemoglobin provides additional properties which are absent from monomeric myoglobin

A

Quaternary structure

67
Q

What are the two general types of proteins?

A

Globular and Fibrous Proteins

68
Q

Among the 5 globular proteins what are the 2 heme proteins

A

Myoglobin and Hemoglobin

69
Q

What are the two substances that confer ability to these heme proteins to transport and store oxygen.

A

Heme and Ferrous Ion

70
Q

Heme and Ferrous Ion are two substances that confer ability to the heme proteins in what process?

A

transport and store oxygen.

71
Q

Heme is a ___ ___ linked by methylene bridges

A

Cyclic tetrapyrrole

72
Q

Heme is a cyclic tetrapyrrole linked by ____

A

Methylene bridges

73
Q

Ferrous ion resides at the ____ of the planar ring

A

Center

74
Q

Ferrous ion resides at the center of the ____

A

planar ring

75
Q

The _____ of ferrous to ferric ion destroys the biological activity of heme proteins.

A

Oxidation

76
Q

The oxidation of ___ to ___ destroys the biological activity of heme proteins.

A

ferrous, ferric ion

77
Q

The oxidation of ferrous to ferric ion destroys the _____ of ____.

A

biological activity, heme proteins

78
Q

Myoglobin is found in red muscles which serves as _____ in times of oxygen deprivation

A

Reservoir

79
Q

Myoglobin is found in red muscles which serves as reservoir in times of ___

A

Oxygen deprivation

80
Q

Myoglobin can only bind to ___ ____ ____.

A

One oxygen molecule

81
Q

Cooperative binding is exhibited in what protein?

A

Globular: Hemoglobin

82
Q

Hemoglobin exhibits what?

A

Cooperative binding

83
Q

What are the three allosteric effects?

A

Heme - heme interactions
Bohr Effect
Effects of 2,3-biphosphoglycerate

84
Q

A globular protein that stores oxygen

A

Myoglobin

85
Q

A globular protein that supplies oxygen

A

Hemoglobin

86
Q

What allosteric effect us the ability of hemoglobin to reversibly bind oxygen which is affected by pO2

A

Heme-Heme Interactions

87
Q

In short, when oxygen, if combined to one of the heme, the other hemes _____ to accept oxygen.

A

Activate

88
Q

Hemoglobin has an increasing affinity for

A

O2

89
Q

The allosteric effect: binding of O2 in hemoglobin drives the release of CO2

A

Bohr effect

90
Q

The bohr effect is depended upon the _____ between the hemes of the hemoglobin tetramer

A

Cooperative interactions

91
Q

In short, when oxygen binds with the heme, ____ will be detached

A

Carbon dioxide

92
Q

In this case, carbon dioxide leaves in our body thru ____

A

Exhaling

93
Q

High altitudes have a ___ __ of O2

A

Low pressure

94
Q

Tends to have simple, regular, and linear structures

A

Fibrous proteins

95
Q

What is the shape of fibrous protein?

A

Elongated shape

96
Q

A collagen fiber consists of three polypeptide chains wrapped around each other in a _____ or triple helix

A

Ropelike twist

97
Q

A collagen fiber consists of ___ ___ ___ wrapped around each other in a ropelike twist or triple helix

A

three polypeptide chains

98
Q

A collagen fiber consists of three polypeptide chains wrapped around each other in a ropelike twist or ___ __

A

triple helix

99
Q

The three strands are held together by hydrogen bonds that involves?

A

Hydroxyproline hydroxylysine

100
Q

Collagen is both ____ and ____ linked by covalent bonds

A

Intermolecularly intramolecularly

101
Q

What increases with age?

A

Cross-linking

102
Q

Collagen belongs to ____ structure protein

A

Secondary

103
Q

What belongs to secondary structure protein?

A

Collagen

104
Q

Collagen belongs to secondary ___ ___

A

Structure protein

105
Q

The amino acid sequence of collagen are arranged in a repetitious ____ ____

A

Tripeptide sequence

106
Q

The amino acid sequence of collagen are arranged in a repetitious tripeptide sequence: ___-___-___

A

Gly-X-Y

107
Q

The X in Gly-X-Y can be any ______

A

Amino acid

108
Q

The X in Gly-X-Y can be any amino acids but is frequently a ___

A

Proline

109
Q

The Y in Gly-X-Y is frequently a __ or ___

A

Hydroxyproline hydroxylysine

110
Q

Even if normal collagens are highly stable its connective
tissue is ____ and is constantly being ___
often in response to growth or injury of the tissue

A

Dynamic, remodeled

111
Q

Even if normal collagens are highly stable its connective
tissue is dynamic and is constantly being remodeled
often in response to ___ or ___ __ __ ____

A

growth or injury of the tissue

112
Q

Normal collagens are highly stable molecules having ____ as long as several years

A

Half-lives

113
Q

The structure of collagen as triple helical: Resulted to bonding of the exposed R-groups of
neighboring __ __, thus the aggregations
into a very long fibers.

A

Collagen monomers

114
Q

The structure of collagen as triple helical: Resulted to bonding of the exposed R-groups of
neighboring collagen monomers, thus the ____
into a very long fibers.

A

aggregations

115
Q

The structure of collagen as triple helical: Resulted to bonding of the exposed R-groups of
neighboring collagen monomers, thus the aggregations
into a ___ __ __.

A

very long fibers.

116
Q

The structure of collagen as triple helical: Resulted to bonding of the exposed ___ of
neighboring collagen monomers, thus the aggregations
into a very long fibers.

A

R-groups

117
Q

In short, amount of
collagen will ____
as we grow.

A

decrease

118
Q

In short, amount of
collagen will decrease
as we grow. Thus,
__ and ___
appear in our face, a
proof that skin collagen is depleting

A

wrinkles, fine lines

119
Q

EDS results from deficiency of ___-____ enzymes or from mutations in the amino acid sequence

A

Collagen-processing

120
Q

EDS results from deficiency if collagen-processing enzymes or from ___ in the amino acid sequence

A

mutations

121
Q

EDS results from two things what are these?

A

deficiency of collagen-processing enzymes or from mutations in the amino acid sequence

122
Q

Osteogenesis imperfecta is also known as

A

Brittle bone syndrome

123
Q

OI is a heterogeneous group of ___ disorders

A

Inherited

124
Q

OI is distinguished by bones that easily __ or ___

A

Bend or fracture

125
Q

What are the two common features of the OI disease

A

Retarded wound healing and a rotated and twisted spine that leads to the humped back appearance

126
Q

What is the lethal form of OI

A

Type II

127
Q

The lethal form of OI is when the fractures appear in ___, as revealed by this radiograph of a stillborn fetus

A

Utero

128
Q

The lethal form of OI is when the fractures appear in utero, as revealed by this radiograph of a __ __

A

stillborn fetus

129
Q

Collagen has an elongated, triple-helical structure that places many of its ___ ___ ___ ___ on the surface of the triple helical molecule

A

Amino acid side chains

130
Q

Collagen has an elongated, triple-helical structure that places many of its amino acid side chains on the ___ of the ___ ___ ___.

A

Surface, triple helical molecule

131
Q

Cross-linking increases by?

A

Age

132
Q

In short, amount of
collagen will decrease
as we grow. Thus,
wrinkles and fine lines
appear in our face, a
proof that ____ ___ is depleting

A

Skin collagen

Biochemistry 1 (5 decks)

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