PROTEINS & AMINO ACIDS
問題一覧
1
Amino acids are organic compounds that contain two groups. What are these?
amino group, carboxyl group
2
How many set of different molecules are there in an amino acid in order to build proteins?
20
3
Proteins consist of one or more chains of amino acids that are called?
polypeptide
4
The 20 common amino acids that make up proteins in the body are mostly this type of anomer.
alpha
5
All amino acids in the body are of this isomer.
L
6
This group provides each amino acid with its identity.
R
7
Peptides and proteins are formed when amino acids are joined together by this type of bonds.
amide
8
The amide bond in peptides and proteins formation are called?
peptide bond
9
A dipeptide has ____ amino acids joined together by ____ peptide bond.
two, one
10
If polypeptides:many amino acids, then proteins:more than ____ amino acids.
40
11
Peptide bonds are formed through this reaction.
condensation
12
This is a group of complex organic macromolecules that contain carbon, hydrogen, oxygen, nitrogen, and
usually sulfur.
protein
13
Proteins are linear polymers of amino acids connected by this type of bonds.
peptide
14
TRUE OR FALSE: Proteins are the most important of all biological compounds.
true
15
TRUE OR FALSE: Proteins are diverse abundant class of biomolecules.
true
16
Protein comes from this greek word that means “first of importance”.
proteios
17
This is the percentage constituted by proteins in the dry weight of cells.
50%
18
TRUE OR FALSE: Proteins are not stored, so it must be consumed daily.
true
19
They are the building blocks of protein.
amino acids
20
What amino acid is this?
alanine
21
Three letter code for Tryptophan.
Trp
22
Single letter code for Tyrosine.
Y
23
What type of molecules are most amino acids?
chirals
24
These are carbon atoms that are attached to four different substituents.
chiral carbon centers
25
These anomers are what most amino acids are.
alpha
26
All amino acids in the body are L-isomers, meaning that their amino group is on the
left
27
Amongst all chiral amino acids, this amino acid is the exemption.
glycine
28
This is the simplest amino acid.
glycine
29
This is a secondary amine.
proline
30
Proline identifies as an
imino acid
31
Amino acids have an acid and basic component, making them
amphiprotic
32
Aqueous solutions of amino acids can act as
buffers
33
Amino acids have a positive and negative end, making them
zwitterions
34
Zwitterions are charged
neutral
35
Zwitterions can only exist in a pH that is
specific
36
This is a pH at which amino acids have equal positive and negative charges.
isoelectric
37
This amino acid has a pI of 6.02
isoleucine
38
This amino acid has a pI of 5.41
aspargine
39
This amino acid has a pI of 10.76
arginine
40
Histidine has a pI of
7.59
41
Aspartic acid has a pI of
2.77
42
To form a peptide bond through condensation reaction, this substance must be cleaved off or removed.
water
43
To form a peptide if the amino acid is in zwitterion form, the first thing to do is to remove this substance from the first amino acid.
oxygen
44
To form a peptide if the amino acid is in zwitterion form, the second thing to do is to remove two of this substance from the second amino acid.
hydrogen
45
To form a peptide if the amino acid is uncharged, the first thing to do is to remove one of each of these substances from the first amino acid.
oxygen, hydrogen
46
To form a peptide if the amino acid is uncharged, the second thing to do is to remove one of this substance from the second amino acid.
hydrogen
47
This classification of amino acids have a side chain that is hydrophobic.
nonpolar
48
These amino acids have side chains that can form hydrogen bonds with water, making them hydrophilic, but they do not carry a charge at physiological pH.
polar uncharged
49
These amino acids have side chains that contain a carboxyl group, which can donate a proton, giving them a negative charge at physiological pH.
polar acidic
50
These amino acids have side chains that contain an amino group, which can accept a proton, giving them a positive charge at physiological pH.
polar basic
51
CLASSIFY: leucine
nonpolar
52
CLASSIFY: aspartic acid
polar acidic
53
CLASSIFY: histidine
polar basic
54
CLASSIFY: glutamine
polar uncharged
55
These amino acids cannot be produced by the body.
essential
56
This essential amino acid is responsible for producing tyrosine and formation of neurotransmitters and hormones.
phenylalanine
57
This essential amino acid promotes the repair of tissues and energy prevision. It is a regulatory amino acid that assists with growth and development.
valine
58
This essential amino acid is required to produce serotonin and melatonin, supports the nervous system, and regulates blood sugar.
tryptophan
59
This essential amino acid balances the protein in the body, and helps as well to process fatty acids to prevent liver failure.
threonine
60
This essential amino acid is involved in muscle development and repair, where deficiency in this amino acid may lead to symptoms similar with hypoglycemia.
isoleucine
61
This essential amino acid contains sulphur, helps in processing fats and preventing liver damage in acetaminophen poisoning, and improves wound healing (clotting).
methionine
62
This essential amino acid is important for the regulation of growth and natural development and repair mechanisms of infants. This is responsible for maintaining energy and regulating blood pH, and clotting as well.
histidine
63
This is a semi-essential amino acid that stimulates the release of growth hormone and insulin, as well as enhances male libido.
arginine
64
This amino acid is converted in the body into nitric oxide and cannot be synthesized by pre-term infants.
arginine
65
This essential amino acid helps building a healthy immune system through developing antibodies with its antiviral properties, and assists as well with collagen and muscle tissue formation.
lysine
66
This essential acid is the fourth most concentrated within the muscle, which decreases its wasting and supports its building. It maintains nitrogen balance and energy supply and reduces the risk of atherosclerosis.
leucine
67
These are essential amino acids present in relatively small amounts and are below the amino acid requirements.
limiting amino acid
68
Plant-food sources and gelatin are examples of
limiting amino acids
69
The limiting amino acid in grains, nuts, maize, oats, wheat, and rice.
lysine
70
The limiting acid in wheat and rice.
threonine
71
The limiting amino acid in legumes or beans and wheat.
methionine
72
The limiting amino acid in maize.
tryptophan
73
These are proteins that constitute silk fibers.
fibroin
74
FUNCTION: provide strength to cells and tissue
structure
75
FUNCTION: chief constituents of skin, bones, hair, and nails
structure
76
FUNCTION: enzymes are responsible for speeding up reactions in the body and lowers activation energy
catalysis
77
FUNCTION: muscles are made up of protein molecules
movement
78
This protein regulates the interaction of actin and myosin.
tropomyosin
79
FUNCTION: proteins transport other substances
transport
80
FUNCTION: chemical messengers in the bloodstream
hormones
81
FUNCTION: a protein from an outside source or some other foreign substance (antigen) is counteracted by the body’s own proteins (antibodies)
protection
82
FUNCTION: providing a reservoir of an essential nutrient and sufficient nitrogen in times of need
storage
83
STRUCTURE: This protein structure is in a linear sequence connected by peptide bonds.
primary
84
A small protein has at least ____ amino acid residues.
60
85
STRUCTURE: repetitive conformation of the protein backbone
secondary
86
STRUCTURE: alpha-helix; beta pleated; random coil
secondary
87
STRUCTURE: complete 3D arrangement of the atoms in a protein
tertiary
88
STRUCTURE: spatial relationship and interactions between subunits in a protein that has more than one polypeptide chain
quaternary
89
SHAPE: long and narrow, repetitive amino acid sequences
fibrous
90
SHAPE: mainly for structural purposes
fibrous
91
SHAPE: less sensitive to pH and temperature changes and insoluble in water
fibrous
92
SHAPE: round or spherical, with irregular amino acid sequence
globular
93
SHAPE: takes on a more active role, is sensitive to pH and temperature changes, and soluble to water
globular
94
COMPOSITION: Also called homoproteins, these proteins are composed of amino acids.
simple
95
COMPOSITION: Proteins that contain a prosthetic group or a non-protein part in addition to protein.
conjugated
96
COMPOSITION: Proteins derived from simple or conjugated proteins by physical or chemical means.
derived
97
NUTRITION: Generally coming from animal and fish products, these proteins are said to contain an adequate amount of all the essential amino acids that should be incorporated in the diet in equal proportion.
complete
98
NUTRITION: Also called partial proteins, these are any protein that lack one or more essential amino acids in correct proportion.
incomplete
99
Two incomplete proteins may combine to form a complete protein. The proteins that compensate for each other’s lack of amino acids are proteins that are
complementary
100
This is the loss of the secondary, tertiary and quaternary structures of a protein by a chemical or a physical agent while the primary structure is in tact.
denaturation
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1
Amino acids are organic compounds that contain two groups. What are these?
amino group, carboxyl group
2
How many set of different molecules are there in an amino acid in order to build proteins?
20
3
Proteins consist of one or more chains of amino acids that are called?
polypeptide
4
The 20 common amino acids that make up proteins in the body are mostly this type of anomer.
alpha
5
All amino acids in the body are of this isomer.
L
6
This group provides each amino acid with its identity.
R
7
Peptides and proteins are formed when amino acids are joined together by this type of bonds.
amide
8
The amide bond in peptides and proteins formation are called?
peptide bond
9
A dipeptide has ____ amino acids joined together by ____ peptide bond.
two, one
10
If polypeptides:many amino acids, then proteins:more than ____ amino acids.
40
11
Peptide bonds are formed through this reaction.
condensation
12
This is a group of complex organic macromolecules that contain carbon, hydrogen, oxygen, nitrogen, and
usually sulfur.
protein
13
Proteins are linear polymers of amino acids connected by this type of bonds.
peptide
14
TRUE OR FALSE: Proteins are the most important of all biological compounds.
true
15
TRUE OR FALSE: Proteins are diverse abundant class of biomolecules.
true
16
Protein comes from this greek word that means “first of importance”.
proteios
17
This is the percentage constituted by proteins in the dry weight of cells.
50%
18
TRUE OR FALSE: Proteins are not stored, so it must be consumed daily.
true
19
They are the building blocks of protein.
amino acids
20
What amino acid is this?
alanine
21
Three letter code for Tryptophan.
Trp
22
Single letter code for Tyrosine.
Y
23
What type of molecules are most amino acids?
chirals
24
These are carbon atoms that are attached to four different substituents.
chiral carbon centers
25
These anomers are what most amino acids are.
alpha
26
All amino acids in the body are L-isomers, meaning that their amino group is on the
left
27
Amongst all chiral amino acids, this amino acid is the exemption.
glycine
28
This is the simplest amino acid.
glycine
29
This is a secondary amine.
proline
30
Proline identifies as an
imino acid
31
Amino acids have an acid and basic component, making them
amphiprotic
32
Aqueous solutions of amino acids can act as
buffers
33
Amino acids have a positive and negative end, making them
zwitterions
34
Zwitterions are charged
neutral
35
Zwitterions can only exist in a pH that is
specific
36
This is a pH at which amino acids have equal positive and negative charges.
isoelectric
37
This amino acid has a pI of 6.02
isoleucine
38
This amino acid has a pI of 5.41
aspargine
39
This amino acid has a pI of 10.76
arginine
40
Histidine has a pI of
7.59
41
Aspartic acid has a pI of
2.77
42
To form a peptide bond through condensation reaction, this substance must be cleaved off or removed.
water
43
To form a peptide if the amino acid is in zwitterion form, the first thing to do is to remove this substance from the first amino acid.
oxygen
44
To form a peptide if the amino acid is in zwitterion form, the second thing to do is to remove two of this substance from the second amino acid.
hydrogen
45
To form a peptide if the amino acid is uncharged, the first thing to do is to remove one of each of these substances from the first amino acid.
oxygen, hydrogen
46
To form a peptide if the amino acid is uncharged, the second thing to do is to remove one of this substance from the second amino acid.
hydrogen
47
This classification of amino acids have a side chain that is hydrophobic.
nonpolar
48
These amino acids have side chains that can form hydrogen bonds with water, making them hydrophilic, but they do not carry a charge at physiological pH.
polar uncharged
49
These amino acids have side chains that contain a carboxyl group, which can donate a proton, giving them a negative charge at physiological pH.
polar acidic
50
These amino acids have side chains that contain an amino group, which can accept a proton, giving them a positive charge at physiological pH.
polar basic
51
CLASSIFY: leucine
nonpolar
52
CLASSIFY: aspartic acid
polar acidic
53
CLASSIFY: histidine
polar basic
54
CLASSIFY: glutamine
polar uncharged
55
These amino acids cannot be produced by the body.
essential
56
This essential amino acid is responsible for producing tyrosine and formation of neurotransmitters and hormones.
phenylalanine
57
This essential amino acid promotes the repair of tissues and energy prevision. It is a regulatory amino acid that assists with growth and development.
valine
58
This essential amino acid is required to produce serotonin and melatonin, supports the nervous system, and regulates blood sugar.
tryptophan
59
This essential amino acid balances the protein in the body, and helps as well to process fatty acids to prevent liver failure.
threonine
60
This essential amino acid is involved in muscle development and repair, where deficiency in this amino acid may lead to symptoms similar with hypoglycemia.
isoleucine
61
This essential amino acid contains sulphur, helps in processing fats and preventing liver damage in acetaminophen poisoning, and improves wound healing (clotting).
methionine
62
This essential amino acid is important for the regulation of growth and natural development and repair mechanisms of infants. This is responsible for maintaining energy and regulating blood pH, and clotting as well.
histidine
63
This is a semi-essential amino acid that stimulates the release of growth hormone and insulin, as well as enhances male libido.
arginine
64
This amino acid is converted in the body into nitric oxide and cannot be synthesized by pre-term infants.
arginine
65
This essential amino acid helps building a healthy immune system through developing antibodies with its antiviral properties, and assists as well with collagen and muscle tissue formation.
lysine
66
This essential acid is the fourth most concentrated within the muscle, which decreases its wasting and supports its building. It maintains nitrogen balance and energy supply and reduces the risk of atherosclerosis.
leucine
67
These are essential amino acids present in relatively small amounts and are below the amino acid requirements.
limiting amino acid
68
Plant-food sources and gelatin are examples of
limiting amino acids
69
The limiting amino acid in grains, nuts, maize, oats, wheat, and rice.
lysine
70
The limiting acid in wheat and rice.
threonine
71
The limiting amino acid in legumes or beans and wheat.
methionine
72
The limiting amino acid in maize.
tryptophan
73
These are proteins that constitute silk fibers.
fibroin
74
FUNCTION: provide strength to cells and tissue
structure
75
FUNCTION: chief constituents of skin, bones, hair, and nails
structure
76
FUNCTION: enzymes are responsible for speeding up reactions in the body and lowers activation energy
catalysis
77
FUNCTION: muscles are made up of protein molecules
movement
78
This protein regulates the interaction of actin and myosin.
tropomyosin
79
FUNCTION: proteins transport other substances
transport
80
FUNCTION: chemical messengers in the bloodstream
hormones
81
FUNCTION: a protein from an outside source or some other foreign substance (antigen) is counteracted by the body’s own proteins (antibodies)
protection
82
FUNCTION: providing a reservoir of an essential nutrient and sufficient nitrogen in times of need
storage
83
STRUCTURE: This protein structure is in a linear sequence connected by peptide bonds.
primary
84
A small protein has at least ____ amino acid residues.
60
85
STRUCTURE: repetitive conformation of the protein backbone
secondary
86
STRUCTURE: alpha-helix; beta pleated; random coil
secondary
87
STRUCTURE: complete 3D arrangement of the atoms in a protein
tertiary
88
STRUCTURE: spatial relationship and interactions between subunits in a protein that has more than one polypeptide chain
quaternary
89
SHAPE: long and narrow, repetitive amino acid sequences
fibrous
90
SHAPE: mainly for structural purposes
fibrous
91
SHAPE: less sensitive to pH and temperature changes and insoluble in water
fibrous
92
SHAPE: round or spherical, with irregular amino acid sequence
globular
93
SHAPE: takes on a more active role, is sensitive to pH and temperature changes, and soluble to water
globular
94
COMPOSITION: Also called homoproteins, these proteins are composed of amino acids.
simple
95
COMPOSITION: Proteins that contain a prosthetic group or a non-protein part in addition to protein.
conjugated
96
COMPOSITION: Proteins derived from simple or conjugated proteins by physical or chemical means.
derived
97
NUTRITION: Generally coming from animal and fish products, these proteins are said to contain an adequate amount of all the essential amino acids that should be incorporated in the diet in equal proportion.
complete
98
NUTRITION: Also called partial proteins, these are any protein that lack one or more essential amino acids in correct proportion.
incomplete
99
Two incomplete proteins may combine to form a complete protein. The proteins that compensate for each other’s lack of amino acids are proteins that are
complementary
100
This is the loss of the secondary, tertiary and quaternary structures of a protein by a chemical or a physical agent while the primary structure is in tact.
denaturation