Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochemistry > Proteins > Flashcards

Proteins Flashcards

1
Q

The most abundant and functionally diverse molecules in living systems

A

Proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Only amino acid that doesn’t have primary amino group but a secondary amino group

A

Proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Amino acid with this R group fill up the interior of the folded protein and help give it its three-dimensional shape.

A

nonpolar R groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Results from the replacement of polar glutamate with nonpolar valine at the sixth position in the β subunit of hemoglobin

A

Sickle cell anemia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Imino acid

A

Proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

The side chain and α-amino N of this amino acid form a rigid, five-membered ring structure

A

Proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

The side chain of cysteine contains a ________, which is an important component of the active site of many enzymes.

A

sulfhydryl (thiol) group (–SH)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Two disulfide-linked cysteines are referred to as

A

cystine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

4 amino acids with acidic side chains

A

Aspartate
Glutamate
Asparagine
Glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

3 amino acids with basic side chains

A

Lysine
Arginine
Histidine (weakly basic)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

The only amino acid with a side chain that can ionize within the physiologic pH range

A

Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Amino acid with abbreviation of R

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Amino acid with abbreviation of N

A

Asparagine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Amino acid with abbreviation of D

A

Aspartate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Amino acid with abbreviation of E

A

Glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Amino acid with abbreviation of Q

A

Glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Amino acid with abbreviation of F

A

Phenylalanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Amino acid with abbreviation of Y

A

Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Amino acid with abbreviation of W

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Amino acid with abbreviation of K

A

Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

The only amino acid that is not chiral or optically active

A

Glycine (only 2 hydrogen substituents while the rest has 4)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

All amino acids found in proteins are of what configuration

A

L configuration

However, D-amino acids are found in some antibiotics and in bacterial cell walls.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Substances such as amino acids that can act either as an acid or a base are defined as

A

amphoteric and are referred to as ampholytes (amphoteric electrolytes)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

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

A

Poteome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

5 amino acids with aliphatic or nonpolar side chains

A 
Glycine
Alanine
Valine
Leucine
Isoleucine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

3 amino acid containing OH groups

A

Serine
Threonine
Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

2 amino acids containing sulfur atoms

A

Cysteine

Methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

5 amino acids with aromatic side chains

A 
Histidine
Phenylalanine
Tyrosine
Tryptophan (double ring)
Proline
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Amino acid that has the smallest side chain

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Amino acid that carries nitrogen from peripheral tissues to the liver

A

Alanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Amino acid with the largest side chain

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Tryotophan is precursor of what 3 substances/hormones

A

Niacin
Serotonin
Melatonin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Precursor of homocysteine

A

Methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

Amino acid that contributes to the fibrous structure of collagen and interrupts alpha-helices in globular proteins

A

Proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Amino acid which is the phosphorylation site of enzyme modification

A

Serine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

2 amino acids that are sites for O-linked glycosylation in Golgi apparatus

A

Serine

Threonine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Amino acid site for N-linked glycosylation in ER

A

Asparagine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Precursor of glutathione

A

Glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Amino acid that is used in diagnosis of folic acid deficiency

A

Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Individuals deficient in folic acid excrete increased amounts of __________ in urine, particularly after ingestion of large doses of histidine

A

N-formiminoglutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Precursor of creatinine, urea, and NO

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

21st amino acid

A

Selenicysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

Amino acid formed when A selenium atom replaces the sulfur of its structural analog, cysteine

A

Selenocysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

Defined as an atom in a molecule that is bonded to 4 different chemical species allowing optical isomerism

A

Chiral center

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Chemical compound that has a total net charge of zero

A

Zwitterion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Which group in the amino acid accepts protons?

A

Amino group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Which group in the amino acid donates protons?

A

Carboxylic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Essential amino acids

A

PVT TIM HALL, always ARGues, never TYRes

Phenylalanine
Valine
Tryptophan
Threonine
Isoleucine
Methionine
Histidine
Arginine
Leucine
Lysine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

Linear sequence of a protein’s amino acids

A

Primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Sanger’s reagent

A

1-fluoro-2,4-dinitrobenzene

Acts on N-terminal

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Edman’s reagent

A

Phenylisothiocyanate

Acts on N-terminal

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

The folding of short contiguous segments of polypeptide into geometrically ordered units

A

Secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Secondary structure is stabilized by

A

Hydrogen bonding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Most common secondary structure

A

Alpha helix

55
Q

How many AA per turn of the spiral in alpha helix?

A

3.6

56
Q

3 structures that disrupts the alpha helix

A

Proline
Large R-groups
Charged R-groups

57
Q

Secondary structure in keratin

A

100% alpha helix

58
Q

Secondary structure in hemoglobin

A

80% alpha helix

59
Q

Secondary structure in amyloid

A

Beta pleated sheet

60
Q

Secondary structure in immunoglobulin

A

Beta pleated sheet

61
Q

Refers to the folding of domains and their final arrangement

A

Tertiary structure

62
Q

4 interactions that stabilize the tertiary structure of proteins

A

Disulfide bond
Hydrogen bond
Hydrophobic bond
Ionic bond

63
Q

Fundamental functional and 3-dimensional structural units of a polypeptide

A

Domains

Formed by combinations of motifs

64
Q

Specialized group of proteins required for the proper folding of many species of proteins

A

Chaperones

65
Q

Can rescure proteins that have become thermodynamically trapped in a misfolded dead end by unfolding hydrophobic regions

A

Chaperones

66
Q

Structure of proteins consisting of more than one polypeptide chain

A

Quaternary structure

67
Q

Fatal neurodegenerative diseases characterized by spongiform changes, astrocytic gliomas, and neuronal loss resulting from the deposition of insoluble protein aggregates in neural cells

A

Prion diseases

68
Q

Prion disease in cannibalistic tribe

A

Kuru

69
Q

Normal protein in prion disease

A

PrPc, rich in alpha-helices

70
Q

Abnormal protein in prion disease

A

PrPsc, rich in beta sheet

71
Q

Form of hemoglobin that has low oxygen affinity

A

Taut form

72
Q

Form of hemoglobin that has high oxygen affinity

A

Relaxed form

73
Q

Amino acid that plays a role in O2 binding in myoglobin

A

Histidine

74
Q

Heme protein that consist of a single polypeptide chain composed of polar and non-polar AAs, and is a reservoir of O2

A

Myoglobin

75
Q

O2 dissociation curve of hemoglobin

A

Sigmoidal

76
Q

O2 dissociation curve of myoglobin

A

Hyperbolic

77
Q

Increase in P50 will shift the O2 dissociation curve to the

A

Right

78
Q

Decrease in P50 will shift the O2 dissociation curve to the

A

Left

79
Q

The deoxygenated form of hemoglobin has a greater affinity for protons than does oxyhemoglobin. What do you call this effect?

A

Bohr effect

80
Q

A condition when there is “Chocolate” cyanosis or blood is a muddy brown color; with 85% O2 saturation

A

Methemoglobinemia

81
Q

Treatment of methemoglobinemia

A

Methylene blue

Or ascorbic acid if mild

82
Q

Hemoglobin that contains 2 alpha chains and 2 gamma-chains

A

Fetal hemoglobin

83
Q

Disorder characterized by an inherited defect in the RBC membrane that renders the erythrocytes spheroidal, less deformable, and vulnerable to splenic sequestration

A

Hereditary spherocytosis

84
Q

Diagnostic test for hereditary spherocytosis

A

Osmotic fragility test

85
Q

Hemoglobin variant that has a single amino acid substitution in the 6th position of the beta-globin, in which lysine is substituted for glutamate

A

Hemoglobin C disease

86
Q

What accumulates in alpha thalassemia?

A

Beta chains

87
Q

What accumulates and precipitates in beta thalassemia?

A

Hb Barts accumulates

Alpha chain precipitates

88
Q

Absence of 1 alpha globin gene

A

Silent carrier

89
Q

Absence of 2 alpha globin gene

A

Alpha-thalassemia

90
Q

Absence of 3 alpha globin gene

A

Hemoglobin H disease

91
Q

Absence of 4 alpha globin gene

A

Hydrops fetalis

92
Q

Most abundant protein in the body

A

Collagen

93
Q

A long stiff extracellular structure in which 3 polypeptides (alpha-chain) each 1000 AA in length are wound around one another in a triple helix

A

Collagen

94
Q

Most common type of collagen

A

Type 1

95
Q

Collagen is rich in what 2 amino acids?

A

Glycine and proline

Also hydroxyproline and hydroxylysine

96
Q

Type of collagen in the bone

A

Type 1

97
Q

Type of collagen in the cornea

A

Type 1

98
Q

Type of collagen in late wound repair

A

Type 1

Also found in bone, skin, tendon, dentin, fascia, cornea

99
Q

Type of collagen in the cartilage

A

Type 2

100
Q

Type of collagen in the vitreous body

A

Type 2

101
Q

Type of collagen in the nucleus pulposus

A

Type 2

102
Q

Type of collagen in the blood vessels

A

Type 3

103
Q

Type of collagen in the fetal tissue

A

Type 3

104
Q

Type of collagen in the granulation tissue

A

Type 3

Also in skin, blood vessels, uterus, fetal tissues

105
Q

Type of collagen in the basement membrane and basal lamina

A

Type 4

106
Q

Most frequently affected collagen in Ehlers-Danlos Syndrome

A

Type 3

107
Q

Results from inheritable defects in the metabolism of fibrillar collagen

A

Ehlers-Danlos Syndrome

108
Q

Hyperextendable skin, tendency to bleed, hypermobile joints, with increased risk for berry aneurysms

A

Ehlers-Danlos syndrome

109
Q

Mutation in collagen genes resulting to bones that easily bend and fracture

A

Osteogenesis imperfecta

110
Q

Most common mode of inheritance of osteogenesis imperfecta

A

Autosomal dominamy

111
Q

Collagen that is abnormal in osteogenesis imperfecta

A

Type 1

112
Q

Multiple fractures, blue sclerae, hearing loss, dental imperfections

A

Osteogenesis imperfecta

113
Q

Sore spongy gums, loose teeth, poor wound healing and petechiae on skin and mucous membranes

A

Scurvy

114
Q

Collagen affected in Alport’s syndrome

A

Type 4

115
Q

A number of genetic disorders affecting the structure of type 4 collagen fibers

A

Alport’s syndrome

116
Q

Characterized by kinky hair and growth retardation; reflects a dietary deficiency of the copper

A

Menke’s syndrome

117
Q

Mutations affecting the structure of Type VII collagen, which forms delicate fibrils that anchor the basal lamina to collagen fibrils in the dermis; the skin breaks and blisters as a result of minor trauma

A

Epidermolysis bullosa

118
Q

Elastine is rich in what 2 amino acids

A

Proline and lysine

Little hydroxyproline
No hydroxylysine

119
Q

Mutation in the fibrillin gene

A

Marfan syndrome

120
Q

Mode of inheritance of Marfan Symdrome

A

Autosomal dominant

121
Q

Rigidity of keratin is determined by the number of ________

A

disulfide bonds

122
Q

Secondary structure that reverse the direction of a polypeptide chain, helping it form a compact, globular shape

A

β-Bends

123
Q

Refers to the disordered structure obtained when proteins are denatured

A

“random coil”

124
Q

Globular proteins are constructed by combining secondary structural elements, producing specific geometric patterns or

A

motifs

125
Q

The information needed for correct protein folding is contained in the what structure of the polypeptide

A

primary

126
Q

Chaperones are also known as

A

Heat shock proteins

127
Q

Cage-like chaperones

A

Chaperonins

128
Q

Proteins that perform the same function but have different primary structures

A

Isoforms

129
Q

Long, fibrillar protein assemblies consisting of β-pleated sheets; insoluble, spontaneously aggregating proteins

A

amyloids

130
Q

The accumulation of neurofibrillary tangles inside neurons. A key component of these tangled fibers is an abnormal form (hyperphosphorylated and insoluble) of the tau (τ) protein

A

Alzheimer disease

131
Q

The most common causeof familial Alzheimer Disease is a mutation in what gene

A

presenilin, catalytic subunit of gamma-secretase

132
Q

The causative agent of transmissible spongiform encephalopathies (TSEs)

A

prion protein (PrP)

133
Q

Histones are rich in what 2 amino acids?

A

Lysine

Arginine

Biochemistry (6 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions