Brainscape's Knowledge GenomeTM

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


See full index

Chemistry Ni Ma'am R > FINAL TERM > Flashcards

FINAL TERM Flashcards

You may prefer our related Brainscape-certified flashcards:
Chemistry 101 flashcards AP® Chemistry flashcards Periodic Table flashcards Organic Chemistry 101 flashcards
1
Q

Class of Protein

A

Structural, Contractile, Transport, Storage, Hormone, Enzyme, and Protection

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

Class of Protein that regulate body metabolism and nervous system

A

Hormone

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

Class of protein that catalyze biochemical reactions in the cells

A

Enzyme

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

Class of protein that recognizes and destroy foreign substances

A

Protection

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

-are the building blocks of proteins
-contain a carboxylic acid group and an amino group
-on the alpha (α) carbon
-are ionized in solution
-each contains a different side group (R)

A

Amino acids

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

Types of Amino acids

A

Polar, nonpolar, acidic, and basic

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

Type of amino acids with hydrocarbon
side chains (hydrophobic)
-has an R group that is H, an
alkyl group, or aromatic.

A

Nonpolar

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

Type of amino acids with polar
or ionic side chains
(hydrophilic)
-has an R group that is alcohol,
thiol, or amide.

A

Polar (neutral)

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

Type of amino acids with
–NH2 side chains
(hydrophilic)
-with an amino R group (NH3+)

A

Basic

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

-are chiral except glycine, which has two H atoms
-attached to the alpha carbon atom
-have Fischer projections that are stereoisomers
-that are L isomers are used in proteins

A

Amino acids

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

-has an equal number of —NH3+ and COO– groups
-forms when the H from —COOH in an amino acid
transfers to the —NH2

A

Zwitterion

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

-are the pH at which zwitterions
have an overall zero charge
-of nonpolar and polar (neutral)
amino acids exist at pH values
from 5.1 to 6.3

A

Isoelectric points (pI)

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

the zwitterion accepts a proton
(H) to form a positively charged ion.

A

Acidic solution

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

-In solutions that are more acidic than the pI,
-the COO– in the zwitterion accepts a proton
-the amino acid has a positive charge

A

Zwitterions in Acidic solutions

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

-In solutions that are more basic than the pI,
-the NH3+ in the zwitterion loses a proton
-the amino acid has a negative charge

A

Zwitterions in basic solutions

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

the -NH3+ of the zwitterion loses a
proton, and a negatively charged species is formed.

A

Basic solution

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

-a polar (acidic) amino acid,
-has a pI of 2.8
-forms a zwitterion at pH 2.8
-forms negative ions with charges 1– and 2– at pH
values greater than pH 2.8

A

Aspartic acid

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

-an electric current is used to
separate a mixture of amino acids, and
-the positively charged amino acids move toward the
negative electrode
-the negatively charged amino acids move toward the
positive electrode
-an amino acid at its pI does not migrate
-the amino acids are identified as separate bands on the
filter paper or thin layer plate

A

Electrophoresis

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

-is an amide bond
-forms between the carboxyl group of one amino acid
and the amino group of the next amino acid
-contains an N (free H3N+) terminal written on the left
-contains a C (free COO –) terminal written on the right

A

Peptide bond

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

-a yl ending for the N-terminal (free H3N+) amino acid
-the full amino acid name of the free carboxyl group
(COO–) at the C-terminal end

A

Dipeptide

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

The primary structure of a protein is

A

-the particular sequence of amino acids
-the backbone of a peptide chain or protein

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

-have similar primary structures
-differ only in the amino acids at positions 3 and 8

A

Nonapeptides oxytocin and vasopressin

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

-was the first protein to have
its primary structure
determined
-has a primary structure of
two polypeptide chains
linked by disulfide bonds
-has an A chain with 21
amino acids and a B chain
with 30 amino acids

A

Insulin

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

-a coiled shape held in place by hydrogen bonds
between the amide groups and the carbonyl groups
of the amino acids along the chain
-hydrogen bonds between the H of an —NH group
and the O of C═O of the fourth amino acid down
the chain

A

Alpha helix (α-helix)

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

is a secondary structure that consists of polypeptide chains arranged side by side
-has hydrogen bonds between chains
-has R groups above and below the sheet
-is typical of fibrous proteins such as silk

A

Beta-pleated sheet (β-pleated sheet)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

-consists of three alpha helix
chains woven together
-contains large amounts of
glycine, proline, hydroxyproline,
and hydroxylysine that contain
–OH groups for hydrogen
bonding
-is found in collagen, connective
tissue, skin, tendons, and
cartilage

A

Triple helix

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

are the ten amino
acids not synthesized
by the body

must be obtained from
the diet

are in meat and diary
products

are missing (one or
more) in grains and
vegetables

A

Essential amino acids

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

gives a specific three-dimensional shape to the
polypeptide chain

involves interactions and cross-links between
different parts of the peptide chain

is stabilized by:

hydrophobic and hydrophilic interactions
salt
bridges

hydrogen bonds

disulfide bonds

A

Tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Interactions between nonpolar groups

A

Hydrophobic interactions

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

Attraction between polar and ionized groups and water on the surface of the tertiary structure

A

Hydrophilic interactions

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

Ionic interactions between ionized acidic and basic amino acids

A

Salt bridges

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

Occur between H and O or N

A

Hydrogen bonds

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

Strong covalent links between sulfur atoms of two cysteine amino acids

A

Disulfide bonds

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

have compact,
spherical shapes

carry out synthesis,
transport, and
metabolism in the cells

such as myoglobin
store and transport
oxygen in muscle

A

Globular proteins

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

consist of long, fiber-like
shapes

such as alpha keratins make
up hair, wool, skin, and nails

such as feathers contain
beta keratins with large
amounts of beta-pleated
sheet structures

A

Fibrous proteins

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

is the combination of two or
more tertiary units

is stabilized by the same
interactions found in tertiary
structures

of hemoglobin consists of two
alpha chains and two beta
chains with heme groups in
each subunit that pick up
oxygen for transport in the
blood to the tissues

A

Quaternary structure

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

splits the peptide bonds to give smaller peptides
and amino acids

occurs in the digestion of proteins

occurs in cells when amino acids are needed to
synthesize new proteins and repair tissues

A

Protein hydrolysis

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

the disruption of bonds in the secondary, tertiary,
and quaternary protein structures

heat and organic compounds that break apart H
bonds and disrupt hydrophobic interactions

acids and bases that break H bonds between polar R
groups and disrupt ionic bonds

heavy metal ions that react with S—S bonds to form
solids

agitation, such as whipping, that stretches peptide
chains until bonds break

A

Denaturation

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

an egg is cooked

the skin is wiped with alcohol

heat is used to cauterize

blood vessels

instruments are sterilized in

an autoclave

A

Denaturation

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

are proteins
that

catalyze nearly all the
chemical reactions taking
place in the cells of the
body

increase the rate of
reaction by lowering the
energy of activation

A

Enzymes

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

Classification of enzymes

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

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

Add or remove groups without hydrolysis or oxidation that may result in a double bond

A

Lyases

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

Join molecules using ATP energy

A

Ligases

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

is a region within an
enzyme that fits the
shape of the reacting
molecule, called a
substrate

contains amino acid R
groups that bind the
substrate

releases products when
the reaction is complete

A

Active site

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

a substrate attaches to
the active site

an enzyme–substrate
(ES) complex forms

reaction occurs and
products are released

an enzyme (E) is used
over and over

A

enzyme-catalyzed reaction

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

Enzymes may recognize and catalyze

a single substrate

a group of similar substrates

a particular type of bond

A

Enzyme specificity

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

Catalyze one type of reaction for a single substrate

A

Absolute

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

Catalyze one type of reaction for similar substrates

A

Group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

Catalyze one type of reaction for a specific type of bond

A

Linkage

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

the active site has a rigid shape

only substrates with the matching shape can fit

the substrate is the key that fits that lock

A

Lock-and-key model

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

enzyme structure is flexible, not rigid

shapes of enzyme and substrate adjust for best fit at
the active site to improve catalysis of reaction

substrate specificity increases

A

Induced-fit model

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

The active site is
1) the entire enzyme

2) a section of the enzyme

3) the substrate

A

2

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

In the induced-fit model, the shape of the enzyme
when substrate binds

1) stays the same

2) adapts to the shape of the substrate

A

2

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

catalyze the same reaction in different tissues in
the body

can be used to identify the organ or tissue involved
in damage or disease

such as LDH have one form more prevalent in
heart muscle and another form in skeletal muscle
and liver tissue

A

Isoenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

determine the
amount of damage in
tissues

that are elevated
may indicate damage
or disease in a
particular organ

A

Diagnostic enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

are most active at an
optimum temperature
(usually 37°C in
humans)

show little activity at
low temperatures

lose activity at high
temperatures as
denaturation occurs

A

enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

Enzymes in the body have an optimum pH of about

A

7.4

58
Q

are molecules that cause a loss of catalytic activity

prevent substrates from fitting into the active sites

A

Inhibitors

59
Q

Types of Inhibition

A

Reversible and Irreversible

60
Q

Types of Reversible Inhibition

A

Competitive and noncompetitive

61
Q

has a structure that is
similar to that of the
substrate

competes with the
substrate for the active
site

has its effect reversed by
increasing substrate
concentration

A

Competitive inhibitor

62
Q

has a structure that is much
different than the substrate

distorts the shape of the
enzyme, which alters the
shape of the active site

prevents the binding of the
substrate

cannot have its effect
reversed by adding more
substrate

A

Noncompetitive inhibitor

63
Q

A molecule that forms a covalent bond to a part of the active site, permanently preventing substrates from occupying ir.

A

Irreversible Enzyme Inhibitor

64
Q

is a competitive
inhibitor of succinate
dehydrogenase

has a structure that is
similar to succinate

inhibition is reversed
by adding succinate

A

Malonate

65
Q

Identify each description as an inhibitor that is
1) competitive or 2) noncompetitive.

A. increasing substrate reverses inhibition

B. binds to enzyme surface but not to the active site

C. structure is similar to substrate

D. inhibition is not reversed by adding more substrate

A

Identify each description as an inhibitor that is
1) competitive or 2) noncompetitive.

1 A. increasing substrate reverses inhibition

2 B. binds to enzyme surface but not to the active site

1 C. structure is similar to substrate

2 D. inhibition is not reversed by adding more
substrate

66
Q

are inactive forms of enzymes

are activated when one or more peptides are removed

A

Zymogens

67
Q

produced as zymogens in one organ and transported
to another, such as the pancreas, when needed

activated by removing small peptide sections

A

Digestive enzymes

68
Q

an enzyme in a reaction sequence that binds a
regulator substance

A

Allosteric enzyme

69
Q

when it enhances the binding
of substrate and accelerates the rate of reaction

A

Positive regulator

70
Q

when it prevents the binding
of the substrate to the active site and slows down
the rate of reaction

A

Negative regulator

71
Q

a product acts as a regulator

an end product binds with the first enzyme (E1) in
a sequence when sufficient product is present so
shuts down the reaction

A

Feedback control

72
Q

it binds to threonine deaminase, the first enzyme in
the pathway from threonine to isoleucine

a change in the shape of threonine deaminase blocks
the binding of threonine

A

Isoleucine

73
Q

is an active enzyme that
consists only of protein.

A

Simple enzyme

74
Q

is a cofactor that is a small organic
molecule such as a vitamin.

A

coenzyme

75
Q

Identify each enzyme as

1) a simple enzyme

2) an enzyme that required a cofactor

A. requires Mg2+ for hydrolysis of phosphate esters

B. requires vitamin B3 to transfer an acetyl group

C. is active with four polypeptide subunits

A

Identify each enzyme as

1) a simple enzyme

2) an enzyme that required a cofactor

2 A. requires Mg2+ for hydrolysis of phosphate esters

2 B. requires vitamin B3 to transfer an acetyl group

1 C. is active with four polypeptide subunits

76
Q

soluble in aqueous solutions

cofactors for many enzymes

not stored in the body

A

water-soluble vitamins

77
Q

was the first B vitamin identified

is part of the coenzyme thiamin pyrophosphate (TPP)

is used to decarboxylate α-keto carboxylic acids

has a recommended daily allowance (RDA) of 1.2 mg;
deficiencies include fatigue, poor appetite, weight loss,
nerve degeneration, and heart failure

A

Thiamin (Vitamin B1)

78
Q

is found in the coenzymes flavin adenine dinucleotide
(FAD) and flavin mononucleotide (FMN)

is needed for good vision and healthy skin

has an RDA of 1.2–1.8 mg; deficiencies include
dermatitis, dry skin, tongue inflammation, and
cataracts

A

Riboflavin (Vitamin B2)

79
Q

is part of the coenzyme
nicotinamide adenine
dinucleotide (NAD+) involved in
oxidation–reduction reactions

has an RDA of 14–18 mg

deficiency can result in
dermatitis, muscle fatigue, and
loss of appetite

A

Niacin (Vitamin B3)

80
Q

is part of coenzyme A needed for energy
production

is involved in glucose and cholesterol synthesis

has an RDA of 5 mg

deficiency can result in fatigue, retarded growth,
cramps, and anemia

A

Pantothenic acid (Vitamin B5)

81
Q

two forms of vitamin B6, which are converted to the
coenzyme pyridoxal phosphate (PLP)

required in the transamination of amino acids and
decarboxylation of carboxylic acids

has an RDA of 1.3–2.0 mg; deficiency may lead to
dermatitis, fatigue, and anemia

A

Pyridoxine and pyridoxal

82
Q

consists of four pyrrole rings
with a Co2+

is a coenzyme for enzymes
that transfer methyl groups
and produce red blood
cells

has an RDA of 2.0–2.6 μg

deficiencies are pernicious
anemia, nerve damage, and
malformed red blood cells

A

Cobalamin (Vitamin B12)

83
Q

is required in collagen
synthesis and healing of
wounds

has an RDA of 60–95 mg

deficiencies are scurvy,
weakened connective tissue,
slow-healing wounds, and
anemia

A

Ascorbic acid (Vitamin C)

84
Q

is a coenzyme for enzymes that transfer
carboxyl groups

has an RDA of 30 μg

deficiencies include dermatitis, loss of hair,
fatigue, and anemia

A

Biotin

85
Q

consists of pyrimidine, p-aminobenzoic acid, and
glutamate

forms the coenzyme THF used in the transfer of
methyl groups and is involved in the synthesis of
nucleic acids

has an RDA of 400 μg

deficiencies are abnormal red blood cells,
anemia, and poor growth

A

Folic acid (Folate)

86
Q

vitamins A, D, E, and K

soluble in lipids but not in aqueous solutions

stored in the body

important in vision, bone formation, antioxidants, and
blood clotting

A

Fat-soluble vitamins

87
Q

is needed for retinol (vision); synthesis of RNA

has an RDA of 800 μg

deficiencies include night blindness, immune system
repression, and slowed growth

A

Retinol (Vitamin A)

88
Q

is synthesized in skin
exposed to sunlight

regulates the absorption of
phosphorus and calcium
during bone growth

has an RDA of 5–10 μg

deficiency includes
weakened bones

A

Cholecalciferol (Vitamin D)

89
Q

is an antioxidant in cells

may prevent the oxidation of unsaturated fatty acids

is found in whole grains and vegetables

has an RDA of 15 mg

deficiencies are hemolysis and anemia

A

Tocopherol (Vitamin E)

90
Q

Vitamin K1 in plants has a
saturated side chain.

Vitamin K2 in animals has a
long unsaturated side chain.

Vitamin K2 is needed for the
synthesis of zymogens for
blood clotting.

Vitamin K has an RDA of
90–120 μg.

Deficiencies are prolonged
bleeding time and bruising

A

Menaquinon (Vitamin K)

91
Q

Identify each of the following as a water-soluble vitamin
(WS) or fat-soluble vitamin (FS).

A. folic acid

B. retinol (vitamin A)

C. vitamin C

D. vitamin E

E. niacin

A

Identify each of the following as a water-soluble vitamin
(WS) or fat-soluble vitamin (FS)

WS
A. folic acid

FS
B. retinol (vitamin A)

WS
C. vitamin C

FS
D. vitamin E

WS
E. niacin

92
Q

Identify the vitamin associated with each

1) riboflavin (B2)
2) vitamin A

3) vitamin K
4) vitamin D

5) ascorbic acid

A. collagen formation

B. part of the coenzymes FAD and FMN

C. absorption of phosphorus and calcium in bone

D. vision

E. blood clotting

A

Identify the vitamin associated with each

1) riboflavin (B2)
2) vitamin A

3) vitamin K
4) vitamin D

5) ascorbic acid

5 A. collagen formation

1 B. part of the coenzymes FAD and FMN

4 C.absorption of phosphorus and calcium in bone

2 D. vision

3 E. blood clotting

93
Q

molecules that store information for cellular growth
and reproduction

deoxyribonucleic acid (DNA) and ribonucleic acid
(RNA)

A

Nucleic acids

94
Q

large molecules consisting of long chains of
monomers called

A

nucleotides

95
Q

Nucleotides are consist of

A

base with nitrogen

pentose sugar

phosphoryl group

96
Q

The bases in DNA and RNA are

A

pyrimidines C, T, and U

purines A and G

97
Q

in RNA is ribose

in DNA is deoxyribose, with
no O atom on carbon 2′

has carbon atoms numbered
with primes to distinguish them
from the atoms in the bases

A

Pentose sugar

98
Q

has a base linked by a
glycosidic bond to C1′ of
a sugar (ribose or
deoxyribose)

is named by changing
the end of the base
name to osine for
purines and idine for
pyrimidines

A

nucleoside

99
Q

has a phosphoryl group
attached to the C5′ —OH
group of a nucleoside

is named using the name
of the nucleoside followed
by

-5′-monophosphate

A

nucleotide

100
Q

nucleotides are joined by phosphodiester bonds

the 3′ —OH group of the sugar in one nucleotide
forms an ester bond to the phosphate group on the
5′ carbon of the sugar of the next nucleotide

A

Primary structure of nucleic acids

101
Q

has a free 5′-phosphate
group at one end and a free
3′ —OH group at the other
end

is read from the free 5′ end,
using the letters of the
bases

segment shown here is read
as:

5′—A—C—G—T—3′

A

nucleic acid polymer

102
Q

is a single strand of
nucleotides

consists of the bases A,
C, G, and U linked by
3′—5′ ester bonds
between ribose and
phosphate

A

Primary structure of RNA

103
Q

the percentage of adenine (A) is the same as the
percentage of

A

Thymine

104
Q

the percentage of guanine (G) is the same as the
percentage of

A

Cytosine

105
Q

Adenine is always linked by ____ hydrogen bonds to
thymine (A−T)

A

two

106
Q

guanine is always linked by ______ hydrogen bonds
to cytosine (G−C)

A

Three

107
Q

consists of two strands of
nucleotides that form a double
helix structure like a spiral
stair case

has hydrogen bonds between
the bases A–T and G–C

has bases along one strand
that complement the bases
along the other

A

Double helix

108
Q

involves unwinding the DNA

pairing the bases in each
strand with new bases to
form new complementary
strands

producing two new DNA
strands that exactly
duplicate the original DNA

A

DNA replication

109
Q

from the hydrolysis
of each nucleoside
triphosphate

is used to form a
phosphodiester
bond to each new
nucleotide on the
complementary
strand

A

Hydrolysis energy

110
Q

at each open DNA section (called a __________),
DNA polymerase catalyzes the formation of 5′–3′ ester
bonds of the leading strand

A

Replication fork

111
Q

the lagging strand (growing in the 3′–5′ direction) is
synthesized in short sections called

A

Okazaki fragments

112
Q

Match the following:

1) helicase
2) DNA polymerase

3) replication fork
4) Okazaki fragments

A. short segments formed by the lagging strand

B. the starting point for synthesis in unwound DNA

sections

C. the enzyme that unwinds the DNA double helix

D. the enzyme that catalyzes the formation of

phosphodiester bonds of complementary bases

A

Match the following:

1) helicase
2) DNA polymerase

3) replication fork
4) Okazaki fragments

4 A. Short segments formed by the lagging strand.

3 B. The starting point for synthesis in unwound DNA
sections.

1 C. The enzyme that unwinds the DNA double helix

2 D. The enzyme that catalyzes the formation of
phosphodiester bonds of complementary bases

113
Q

transmits information from DNA to make proteins

A

RNA

114
Q

carries genetic information from DNA to the ribosomes.

A

Messenger RNA (mRNA)

115
Q

brings amino acids to the ribosome to make the protein.

A

Transfer RNA (tRNA)

116
Q

makes up 2/3 of ribosomes where protein synthesis takes place.

A

Ribosomal RNA (rRNA)

117
Q

mRNA is formed from a gene on a DNA strand

A

Transcription

118
Q

tRNA molecules bring amino acids to mRNA to build a protein

A

Translation

119
Q

moves along the DNA template in
the 3′–5′ direction to synthesize the corresponding
mRNA

the mRNA is released at the termination point

A

RNA polymerase

120
Q

DNA contains _______ that code for proteins and
_______ that do not code for proteins

A

exons, introns

121
Q

in which the end products
speed up or slow the synthesis of mRNA

A

Feedback control

122
Q

in which high levels of a
reactant induce the transcription process to
provide the necessary enzymes for that reactant

A

Enzyme induction

123
Q

consists of a control site and
structural genes that produce mRNA for lactose
enzymes.

A

lactose operon

124
Q

is a sequence of nitrogenous bases in an mRNA that
determines the amino acid order for the protein

consists of sets of three bases (triplets) along the
mRNA called codons

has a different codon for all 20 amino acids needed
to build a protein

contains codons that signal the “start” and “end” of a
polypeptide chain

A

Genetic code

125
Q

occurs when a synthetase
uses energy from ATP
hydrolysis to attach an
amino acid to a specific
tRNA

prepares each tRNA to
use a triplet called an
anticodon to complement
a codon on mRNA

A

activation of tRNA

126
Q

an mRNA attaches to a ribosome

the start codon (AUG) binds to a tRNA with
methionine

the second codon attaches to a tRNA with the next
amino acid

a peptide bond forms between the adjacent amino
acids at the first and second codons

A

Initiation

127
Q

the first tRNA detaches from the ribosome

the ribosome shifts to the adjacent codon on the
mRNA

a new tRNA/amino acid attaches to the open
binding site

a peptide bond forms, and the empty tRNA
detaches

the ribosome shifts down the mRNA to read the
next codon

A

Translocation

128
Q

a polypeptide with all the amino acids for a protein
is synthesized

the ribosome reaches a “stop” codon: UGA, UAA,
or UAG

there is no tRNA with an anticodon for the “stop”
codons

the polypeptide detaches from the ribosome

A

Termination

129
Q

Match the following:

1) activation
2) initiation

3) translocation
4) termination

A. Ribosomes move along mRNA, adding amino acids
to a growing peptide chain.

B. A completed peptide chain is released.

C. A tRNA attaches to its specific amino acid.

D. A tRNA binds to the AUG codon of the mRNA on the
ribosome.

A

Match the following:

1) activation
2) initiation

3) translocation
4) termination

3 A. Ribosomes move along mRNA, adding amino
acids to a growing peptide chain.

4 B. A completed peptide chain is released.

1 C. A tRNA attaches to its specific amino acid.

2 D. A tRNA binds to the AUG codon of the mRNA on
the ribosome.

130
Q

alters the nucleotide sequence in DNA

results from mutagens such as radiation and
chemicals

produces one or more incorrect codons in the
corresponding mRNA

produces a protein that incorporates one or more
incorrect amino acids

causes genetic diseases that produce defective
proteins and enzymes

A

Mutation

131
Q

a different base substitutes for the proper base in DNA

there is a change in a codon in the mRNA

the wrong amino acid may be placed in the polypeptide

A

Substitution mutation

132
Q

an extra base adds to or is deleted from the normal
DNA sequence

the codons in mRNA and the amino acids are incorrect
from the base change

A

Frame shift mutation

133
Q

Identify each type of mutation as a substitution (S) or
frame shift (F).

A. Cytosine (C) enters the DNA sequence.

B. One adenosine is removed from the DNA

sequence.

C. A base sequence of TGA in DNA changes to TAA.

A

Identify each type of mutation as a substitution (S) or
frame shift (F).

F A. Cytosine (C) enters the DNA sequence.

F B. One adenosine is removed from the DNA
sequence.

S C. A base sequence of TGA in DNA changes to
TAA.

134
Q

a DNA fragment from one organism is combined
with DNA in another

restriction enzymes are used to cleave a gene from
a foreign DNA and open DNA plasmids in Eschericia
coli

DNA fragments are mixed with the plasmids in E.
coli and the ends are joined by ligase

the new gene in the altered DNA produces protein

A

recombinant DNA

135
Q

restriction enzymes cut a DNA sample into smaller
fragments (RFLPs)

the fragments are sorted by size

a radioactive isotope that adheres to certain base
sequences in the fragments produces a pattern on
X-ray film, which is the “fingerprint”

the “fingerprint” is unique to each individual DNA

A

DNA fingerprinting

136
Q

produces multiple copies of a DNA in a short time

separates the sample DNA strands by heating

mixes the separated strands with enzymes and
nucleotides to form complementary strands

is repeated many times to produce a large
sample of the DNA

A

polymerase chain reaction (PCR)

137
Q

are small particles of DNA or RNA that require a
host cell to replicate

cause a viral infection when the DNA or RNA
enters a host cell

are synthesized in the host cell from the viral
RNA produced by viral DNA

A

Viruses

138
Q

a retrovirus, which contains viral RNA but no viral
DNA, enters a cell

the viral RNA uses reverse transcriptase to
produce a viral DNA strand

the viral DNA strand forms a complementary DNA
strand

the new DNA uses the nucleotides and enzymes
in the host cell to synthesize new virus particles

A

Reverse transcription

139
Q

is a retrovirus that infects
T4 lymphocyte cells

decreases the T4 level,
making the immune
system unable to destroy
harmful organisms

is associated with an
increased chance of
developing pneumonia
and skin cancer
associated with AIDS

A

HIV-1 virus

140
Q

Match the following:

1) virus
2) retrovirus

3) protease inhibitor
4) reverse transcription

A. a virus containing RNA

B. small particles requiring host cells to replicate

C. a substance that prevents the synthesis of viral
proteins

D. using viral RNA to synthesize viral DNA

A

Match the following:

1) virus
2) retrovirus

3) protease inhibitor
4) reverse transcription

2 A. a virus containing RNA

1 B. small particles requiring host cells to replicate

3 C. a substance that prevents the synthesis of viral
proteins

4 D. using viral RNA to synthesize viral DNA

Chemistry Ni Ma'am R (4 decks)

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