Brainscape's Knowledge GenomeTM

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


See full index

Cellular and Molecular Biology > Test 1 Review > Flashcards

Test 1 Review Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

How many different amino acids are there?

A

20

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

Long chains of amino acids are called?

A

Polypeptides because they are held together by peptide bonds

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

What is a structural protein?

A

A protein providing the cell with shape and structure

tubulin and actin are examples

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

What do enzymes do?

A

Catalyze covalent bond formation or breakage

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

Transport molecules do what?

A

Carry other molecules or ions

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

What do motor proteins do?

A

Generates movement in cells and tissues

myosin is example

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

What do storage proteins do?

A

store small molecules or ions

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

What do signal proteins do?

A

Store small molecules or ions

insulin-glucose levels

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

What do receptor proteins do?

A

detect signals and transmit them to the cells resonse machinery

insulin receptor

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

what do gene regulatory proteins do?

A

Binds to DNA to switch genes on or off

Latose repressor is example

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

What is a peptide bond?

A

Covalent bond formed when carbon atom from carboxyl group shares and electron from amino group of 2nd amino acid

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

What type of reaction is a peptide bond?

A

A condensation reaction because a molecule of water is eliminated during bond formation

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

What is a polypeptide backbone?

A

Repeating sequence of core atoms N (-N-C-C), and each end is different

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

The C-terminus contains?

A

The free carboxyl group

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

The N-terminus contains?

A

Amino group with nitrogen

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

When hearing the term R-group, what should you think of?

A

R Groups=Side chain

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

What do the N-terminus and C-terminus provide?

A

directionality and polarity to the polypeptide chain, but R-groups give protein distinct characterstics

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

The conformation of a protein is?

A

It’s final folded structure

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

What are the 3 types of covalent bonds?

A

Electrostatic interactions
Hydrogen bonds
Van der Waals Attraction

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

What do hydrophobic interactions do?

A

help proteins fold into small, compact conformations because the non-polar side chains tend to be forced together to minimize disruption of hydrogen bonded network

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

If the factor that caused the protein to become denatured is removed the protein does what?

A

can refold (re-nature) itself back to to it’s stable conformation

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

Prion diseases are caused by?

A

misfolded protein aggregates.

They occur through rare conformational changes where proteins fold abnormally

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

What is the abnormally folded proteins (of prions) called?

A

PrP

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

What is a dimer?

A

Two proteins bound to one another

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

What are chaprone proteins?

A

Proteins that assist partially folded chains and help them fold along most energy favored pathway.
They also can form isolation chambers that allow single polypeptides to fold without risk of forming aggregates

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

Protein aggregates are called?

A

Amyloid fibers

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

A-Helix and B-Sheets are formed using what type of bonds?

A

hydrogen bonds

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

In an A-helix structure, the N-H pf peptide bond is bonded to the?

A

C=O

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

When A-helices interact and intertwine with each other it is referred to as a?

A

coiled-coiled interaction

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

B-sheets allow what?

A

amyloid fibrils and they use them for structural purposes

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

In parallel B-sheets, how do the polypeptides run?

A

N-terminus to C-terminus

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

What is a protein domain

A

any segment of a polypeptide that can fold into a compact structure

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

Primary structure refers to?

A

The linear amino acid

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

Secondary structure refers to?

A

an organization that forms within certain segments of the polypeptide chain

ex. a-helcies and B-sheets

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

Tertiary Structure refers to?

A

the full, three dimensional confomation of the entire polypeptide

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

Quaternary Structure refers to?

A

a complex of more than one polypeptide joined together

Dimers are an example

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

What are the three different protein domains/motifs?

A

a) all alpha helices
b) mixture of alpha helices and beta sheets
c) all beta sheets

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

What are protein families?

A

they consist of proteins that have amino acid sequences and 3-D confomation that closely resemble each other

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

Proteins that contain multiple copies of a single protein subunit are considered ________ and can interact through?

A

symmetrical and can interact through two identical binding or form multiple copies of a single polypeptide chain

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

Globular proteins are?

A

polypeptide chains fold into compact shape like a ball with irregular surface

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

Proteins can assemble into?

A

filaments, sheets, or spheres

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

Protein orientations are affected by?

A

the number of binding sites

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

If a protein has one binding site?

A

it can form a dimer with another identical protein

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

Identical proteins with 2 binding sites will often form?

A

a long helical filament

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

If two identical protein binding sites are oriented properly, the proteins can also form?

A

a sphere or ring like structure

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

Fibrous proteins are?

A

proteins requiring them to span a large distance

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

Collagen forms what protein shape?

A

a triple helix

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

What are the most common covalent cross-link proteins?

A

sulfer-sulfer bonds

disulfide bonds

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

How do disulfide bonds help proteins?

A

they stabilize a favored protein conformation and acts as a “staple” to reinforce the most favored conformation

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

What is a ligand?

A

any substance that is bond by a protein

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

The ability of a protein to bound to bind selectively and with high affinity is due to what?

A

The formation of noncovalent bonds

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

If the binding of the protein and ligand is unfavored what do the molecules do?

A

dissasociate

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

The folding of a polypeptide chain creates a __________ in the protein which allows what to interact with it?

A

cavity; the ligands to interact and bind with it

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

All proteins must bind with _______ to carry out a specific function.

A

ligand

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

What do antibodies do? What do they bind with?

A

Antibodies are Y shaped and have two binding sites for the antigen. They bind extremely tightly with the target molecule and mark it, inactivate it or mark it for distruction

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

What is the active site?

A

the bonding site on the the surface substrate molecule on which an enzyme acts

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

How do enzymes encourage catalysis?

A

A) holding substrates in a precise alignment
B) stablizing charges of substrates
C) alterins bind angles to force into a favorable reaction

58
Q

What is feedback inhibition?

A

an enzyme early in the rxn pathway is inhibited by a late product in that pathway. When large quantites of the final product build up, later producrs bind to earlier enzymes

59
Q

What type of regulation is feedback inhibition?

A

negative

60
Q

What does feedback inhibition trigger?

A

a conformational change

61
Q

What is allosteric inhibition?

A

can adopt two or more slightly different conformations and activity can be regulated by a shift from one to another.
Basically, each ligand will stablize the confirmation that it binds most strongly to in an effort to switch the protein to its most active form

62
Q

What is protein phosphorylation?

A

addition and removal of phosphate groups from specific proteins often occur in response to signals that specify some change in a cell’s state

63
Q

What is the enzyme that is responsible for the addition of the phosphate group?

A

kinase

64
Q

What is the enzyme involved in the reverse process (removal of a phosphate group)?

A

phosphatase

65
Q

GTP binding proteins form?

A

molecular switches, in that the protein is in its active form when GTP is bound, and becomes inactive when GTP hydrolyzes itself into GDP, switching to the inactive conformation

66
Q

Changing __________ conformation of the motor protein to push the protein forward

A

allosteric

67
Q

What is protein phosphorylation?

A

involved the enzyme catalzed transfer of the terminal phosphate group of ATP to the Hydroxyl group on a serine, threonine, or tyrosine chain of a protein

68
Q

What does protein phosphatase do?

A

removes the phosphate group or is responsible for dephosphorylation

69
Q

How can a protein’s structure be determined?

A

by x-ray crystallography

70
Q

Describe “cell line” and explain what that means

A

Cell line refers to cells that are monoculture and are immortal as long as they have specific nutrients

71
Q

“in vitro” comes from?

A

the fact cell culture experiments are not taking place in the whole living organism

72
Q

What does Affinity chromatography can be used to?

A

isolate the binding partners of a protein of interest

73
Q

A deoxyribonucleic acid is defined as?

A

a molecule consisting of two long polynucleotide chains

74
Q

In what year was DNA recognized as the possible carrier of the genetic informaiton?

A

1940

75
Q

How did Rosaline Franklin discover the double helix?

A

she discovered it using X-ray diffraction patterns of crystalline B-form DNA

76
Q

Shortly describe Griffith’s experiment?

A

Living S strain=mouse dead
Living R strain=mouse lived
Heat-killed S strain=mouse lived
Live R strain + Heat-killed S strain=mouse died

Live S strain material was found in the dead mouse upon autopsy, and a year later it was discovered that the main component of the purified substance was DNA

77
Q

Describe the building blocks of DNA-

A

Phosphate + sugar = sugar-phosphate
sugar-phosphate+ nitrogenous base=nucleotide

nucleotide + hydrogen bonded base pairs=DNA

78
Q

Thread-like structures in the eukaryotic cell nucleus that becomes visible as the cell divides…

Describes?

A

Chromosomes

79
Q

The covalent linkage b/w the sugar phosphate backbone forms a?

A

phosphodiester bond

80
Q

Nucleotide=

A

sugar-phosphate covalently linked to a base

81
Q

Nucleoside=

A

sugar covalently linked to a base (no phosphate group)

82
Q

A & G are?

What is their structure like?

A

Purines ***** KNOW THIS JACKI

double ring nitrogenous bases

83
Q

C & T are?

What is their structure like?

A

pyrumidines**KNOW THIS JACKI

single ring nitrogenous bases

84
Q

The 5’ and 3’ positions help provide?

A

directionality and polarity to the polynucleotide chain

85
Q

How many _______ bonds hold together A & T?

How many hold together C & G?

A

hydrogen
A&T=2 bonds
C&G=3 Bonds

86
Q

Why is the 3’ end called 3’?

A

Because the 3’ end carried an unlinked -OH group attachde to the 3’ position of the sugar ring

87
Q

Why is the 5’ end called 5’?

A

the 5’ end carries a free phosphate group attached to the 5’ position on sugar ring

88
Q

DNA is always read in the _____ direction?

A

DNA is always read in the _____ direction?

89
Q

The DNA double helix is _______ handed?

A

right

90
Q

Hershey and Chase-
What was the DNA labelled with?
What did the experiment conclude?

A

p^32

Protein was labelled with S^35 but only DNA p32 entered bacterial cells

91
Q

What is the central dogma of molecular biology?

A

DNA->RNA->PROTEINS

92
Q

A genome contains?

A

The complete set of information in an organisms DNA

93
Q

What is Chromatin?

A

complex of DNA and Protein, total genetic info carried by all chromosomes in a cell or organism

94
Q

How does Chromosome painting work?

A

exposing the chromatin to a collection of fluorescent dye-labeled DNA

95
Q

Ataxia is a mutaion in what chromosome?

What occurs to the chromosome?

A

Chromosome 12

and one chromosome is longer with additional material from chromosome 4

96
Q

What occurs to the chromosomes during interphase?

A

cell is actively expressing its genes and the DNA is replicated

97
Q

What occurs to the chromosomes during mitosis?

A

chromosomes condense, gene expression laregely ceases, and the mitotic spindle forms from microtubules

condensed chromosomes are captured by mitotic spindle and one set of chromosomes is pulled to each end of cell

nuclear envelope forms around each chromosome and cell divides to form two daughter cells

98
Q

How many DNA sequence elements are required for chromosome replication?

A

3

99
Q

Each chromosome has ______________, ______________, and ____________.

A

Each chromosome has multiple origins of replication, one centromere, and two telomeres

100
Q

What occurs during the M phase?

A

centromere attaches the duplicated chromosomes to the mitotic spindle so that one copy/chromosome is distributed to each daughter cells

101
Q

What is a nucleolus?

A

Non-membrane bound structure composed of proteins and nucleic acids found within the nucleus

Most prominate structure in the interphase nucleus

102
Q

Where is heterochromatin located?

A

mainly around the periphery, immediatly under the nuclear envelope.

103
Q

What do nucleosomes contain?

A

DNA wrapped around the core of eight histone molecules

104
Q

What is contained in an INDIVIDUAL nucleosome CORE particle?

A

8 histones-2 molecules each histone H2A, H2b, H3, and H4

The double stranded DNA-147 nucleotide pairs long that winds around this histone octomer

105
Q

What just an overal nucleosome?

A

A nucleosome core particle plus one of its adjacent DNA linders

106
Q

How many times is the 147 nucleotide pairs of DNA wrapped around the nucleosome core?

A

1.7 turns

107
Q

DNA PACKING-

A linker histone (H1) do what?

A

pull nucleosome particles together into the 30-nm fiber

108
Q

DNA PACKING-

Chromatin isolated from interphase nucleus appears as?

A

threats 30-nm thick

109
Q

DNA PACKING-

Histone H1 consists of a globular region plus?

A

a pair of long tails at its C-terminal and N00termainla ends

110
Q

DNA PACKING-

The globular region contrains?

A

an additional 20 base pairs of the DNA where it exits from the nucleosome core

111
Q

Heterochromatin are?

A

More condensed than Euchromatin

112
Q

Protein machines that use the energy of ATP hydrolyisis to change the postion of the DNA wrapped around nucleosome are?

A

Chromatin-remolding complexes

113
Q

How do Chromatin-remoldeling complexes work?

A

by pushing tightly bound DNA as they move along, they loosen underlying DNA, allowing it to become accessible to other proteins

114
Q

What continues (repeating) allows Chromatin-remodeling complexes to loosen nucleosome DNA by pushing it along the histone core?

A

ATP Hydrolysis

115
Q

___________ of nucleosome sliding can decondense (loosen) chromatin.

A

Multiple rounds

116
Q

The __________ ____ __________ of histone tails can dictate how a stretch of chromatin is treated by cells.

A

pattern of modification

117
Q

Each histone cane be modified by the covalent attatchment of a number of different chemical groups including:

A

an acetyl group, a methyl group, or a phosphate

118
Q

Epigenetic modifications are?

A

covalent attachments of different chem. groups that act on chromatin structure, but DO NOT change genetic sequence

119
Q

Where do most modifications occur on histones?

A

the N-terminal tails

120
Q

____________ modifications to the histone tails can attract heterochromatic-specific proteins that preoduce the smae modifications of neighboring protiens.

A

Repressive

121
Q

Repressive modifications allow heterochromatin to spread until it encounters?

A

a DNA barrier sequence that prevent heterochromatin spread

122
Q

Expression of a gene can be altered by?

A

moving it to another location in the genome

123
Q

What is position effect?

A

the activity of a gene depends on its position along a chromosome

124
Q

An ______ chromosome can be inactivated by heterochromatin formation

A

X chromosome

125
Q

Semiconservative replication refers to?

A

each parental strand serves as the template for one new strand, therefore each daughter double helix is composed of of the original strands plus a completely new strand

126
Q

How is the process of DNA replication started?

A

By initiator proteins that bind to the two specific DNA sequences called replication origins.

127
Q

How do initiator proteins begin?

A

by prying/pulling apart the two strands of the double helix by breaking the hydrogen

128
Q

The addition of a deoxyribonucleotide to the _____ end of a polynucleotide chaing is the fundamental reaction by which DNA is synthesixed

A

addition of a deoxyribonucleotide to the 3’ hydroxyl end

129
Q

DNA is synthesized in the _____ direction

A

5’ to 3’ direction

130
Q

How do nucelotides enter the reaction?

A

as nucleoside triphoshates (5-C sugar attached to nitrogenous base and 3 phosphate group

131
Q

What enzyme catalyzes addition of nuceotides to the free 3’ hydroxyl on growing DNA strand

A

DNA polymerase

132
Q

What bond breakage provides a large amount of energy for the polymerization reaction?

A

the phosphoanhydride bond on incoming nucleoside triphosphate

133
Q

At the replication fork, the two newly synthesized strands are of?

A

opposite polarities

134
Q

DNA polymerase can only catalyze the addition of incoming nuclleotides in what direction?

A

the 5’ to 3’ direction adding nucleosides to 3’ end

135
Q

Initially the lagging strand is made of?

A

short DNA strands called Okazaki fragments

136
Q

If an incorrect nucleotide is added to a growing strand what will DNA polymerase do?

A

cleave it from the strand and replace it with the correct nucleotide before continuing

137
Q

What are the Steps of DNA polymerase’s catalyzation of of nuceotides?

A

First, it monitors the base-pairing and only when match is correct does it catalyze the nucelotide addition reaction.

Second, when it does make a mistake, it fixes it through proofreading

138
Q

DNA polymerase contains two sites, what are they fore?

A

It has two seperate sites for DNA synthesis and proofreading

139
Q

Why exactly is DNA only synthesized in the 5’ to 3’ direction?

A

A need for proofreading

If it was synthesized in the other direction removal of a incorrect nucleotide would block the addition of the correct nucleotide and prevent further elongation

140
Q

DNA polymerase cannot-

A

Start a completly new DNA strand

141
Q

Primase is a

A

RNA polymerase

142
Q

How long are RNA Primers

A

10 nucleotides

Cellular and Molecular Biology (5 decks)

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