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Cell Biology > Exam 1 > Flashcards

Exam 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what 3 amino acids can be phosphorylated?

A

serine, threonine, and tyrosine

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2
Q

what is an allosteric interaction?

A

when molecules bind at alternative sites rather than the active sites, still allows them to control the protein and influence it

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3
Q

what happens if you change the pH of a cell?

A

it drastically changes the molecular shape & alters the chemistry of the entire region (area) of the cell

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4
Q

What are the different types of cells?

A

(unicellular) bacteria & yeast
(multicellular) animal & plant
gametes (sex cells)

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5
Q

Are viruses considered to be a living cell? why or why not?

A

no, they’re not considered to be a living cell. this is because viruses have to have a host in order to live and reproduce, whereas animal or plant cells are self replicating and don’t need the DNA of a host to multiply.

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6
Q

What instructions do genes provide?

A

form, function, and behavior of cells and organisms

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7
Q

describe a catalyst.

A

a molecule that can facilitate a chemical reaction without being consumed or changed

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8
Q

what is the reason for cells varying forms and functions?

A

all cells have different jobs within the body, and those different jobs (functions) require a variety of forms. for example, a neuron is used to send out electrical signals to the body and it has a cell body with dendrites protruding from the sides, whereas a skin cell is used as a layer of protection and balance for your body and is a pretty uniform “square” shape

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9
Q

explain central dogma.

A

theory that states that genetic information can only flow one way, and that way is DNA, RNA, and then proteins, or just directly from RNA to proteins

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10
Q

what are the 4 amino acids?

A

adenosine, thymine, guanine, cytosine

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11
Q

what induces the internalization of the COVID-19 virus?

A

the spike proteins binding with ACE2 receptors

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12
Q

animal and plant DNA is located within the nucleus, where is the DNA material in bacteria cells located?

A

it is incorporated within the cytoplasm of the cell

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13
Q

what advancements did the light microscope help to make happen?

A

the discovery of cells and the idea that cell come from other preexisting cells

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14
Q

what cell components did the light microscope reveal?

A

nuclei, cytoplasm, organelles, sub cellular structures, cell ultrastructure, specific molecular locations

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15
Q

chromatic dyes

A

presence of nuclei

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16
Q

interference contrast

A

nuclei, cytoplasm, organelles, sub cellular structures

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17
Q

electron microscope

A

cell ultrastructure

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18
Q

fluorescence microscopy

A

specific molecular locations, subunits composed of fiber, molecules as components of vesicles

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19
Q

why do you have to “embalm”, or remove the water, from cells in electron microscopy and interference contrast?

A

if there is water in the cell the light will refract off of it and wouldn’t allow us to see into the cell

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20
Q

what is resolution?

A

the ability to distinguish between two points

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21
Q

conventional light microscopy

A

allows us to magnify cells up to 1000x and resolve details as small as 200 nm

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22
Q

fluorescence microscopy

A

cells are stained with fluorescent dyes, similar to light microscope except light is passing through two filters (yellow). first filter filters the light, second filter blocks out the light and only allows wavelengths that excite the particular fluorescent dye to reach the specimen, uses “reflective” light and mirror to control wavelength

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23
Q

transmitted light microscopy

A

uses laser light that is transmitted THROUGH the specimen

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24
Q

what kind of cell has a singular circular chromosome?

A

prokaryotic cells

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25
Q

prokaryotic cell features

A

no nuclei
very few compartments
most diverse & numerous cells on Earth
divided into 2 domains: bacteria & archaea

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26
Q

eukaryotic cell components

A

nucleus, mitochondria, chloroplast, internal membrane, cytosol, cytoskeleton

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27
Q

nucleus

A

stores information

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28
Q

mitochondria

A

generates useable energy from food molecules

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29
Q

chloroplast

A

capture energy from sunlight

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30
Q

internal membrane

A

creates intracellular compartments all with different functions

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31
Q

cytosol

A

concentrated aqueous gel that contains large and small molecules, highly dynamic (not static)

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32
Q

cytoskeleton

A

responsible for directed cell movement

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33
Q

what is chromatin and where is it located within the cell?

A

DNA & associated structural proteins, it is located in the nucleus

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34
Q

what are the two types of chromatin and what are their characteristics?

A

heterochromatin: condensed, packed, genes less available for expression
euchromatin: dispersed, open form, open for gene expression

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35
Q

what are the prokaryotic qualities of the mitochondria?

A

has independent genetic system
contains circular DNA
contains ribosomes that are more similar to prokaryotic ribosomes than eukaryotic

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36
Q

why does the mitochondria have a convoluted inner membrane?

A

it contains proteins for energy production, the convoluted inner membrane gives the cell more surface area for energy production

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37
Q

smooth endoplasmic reticulum function

A

stores lipids and proteins, not decorated with ribosomes

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38
Q

rough endoplasmic reticulum function

A

site of protein synthesis for proteins destined for secretion or membrane proteins, studded with ribosomes

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39
Q

symbiosis theory: the origin of the mitochondria

A

suggests that mitochondria are descended from specialized bacteria that somehow survived endocytosis by another species of prokaryote or some other cell type and became incorporated into the cytoplasm

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40
Q

Golgi apparatus functions

A

site of molecular sorting
packaging and modifying proteins & lipids destined for specialized regions of the cell
site of glycosylation

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41
Q

what is glycosylation?

A

carbohydrate modification of of proteins and lipids

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42
Q

cytoskeleton function and structure

A

composed of three major filament systems
required for structural maintenance of compartments: ER, Golgi, etc
responsible for directed movements, cell shape, and cell motility

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43
Q

what are the 3 different types of cytoskeleton filaments?

A

actin, microtubules, and intermediate filaments

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44
Q

microtubule function

A

reorganized to form mitotic spindles to segregate chromosomes in a dividing animal cell

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45
Q

what particle tells us atomic number?

A

protons

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46
Q

what part of a fatty acid chain carries the charge?

A

the carboxylic head carries the charge

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47
Q

why are all amino acids different

A

they all have different R groups

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48
Q

what are nucleotides made up of?

A

5 carbon sugar, base, and ribonucleic acid (RNA) or deoxyribonucleic acid (DNA)

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49
Q

what kind of impact do bonds have one molecules?

A

they impact how they bond with water and the shape of the molecule

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50
Q

can regional affects happen without any significant changes?

A

yes

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51
Q

how are macromolecules formed?

A

polymer formed from small molecules, like monomers, that are linked together by covalent bonds

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52
Q

what gives you the primary structure of macromolecules?

A

polymerization of the molecular subunits

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53
Q

will upping the charge in a cell disassemble a hydrophobic tail?

A

no, because hydrophobic regions run from charge in a cell

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54
Q

what kind of interaction can mediate between a macromolecule and a small molecule?

A

non covalent bonds

55
Q

what does a longer half life mean for non covalent reactions?

A

it means they will take longer to dissociate

56
Q

what competes water off of proteins and why?

A

things like glycerol will compete water off of proteins, this will allow the protein to have a higher chance of polymerization

57
Q

can molecules with a lot of charge groups & polarity interact with water without their cells polymerizing?

A

yes

58
Q

What do hydrocarbons associate with?

A

they don’t interact with water, they associate with other like non polar, hydrophobic molecules and will ultimately be displaced (oil slick on top of water)

59
Q

what drives hydrophobic reactions within cells?

A

the collision energy of water

60
Q

what kind of interactions give you a bilayer membrane?

A

tail to tail interactions

61
Q

what do polysaccharides do for a cell?

A

there are a place of major storage and a structural entity used by all cells

62
Q

what is glycogen?

A

storage form of energy in the liver of animals, is a long chain of sugars regulated by insulin

63
Q

why are polysaccharides important for cells?

A

cell cell recognition, communication, and how cells interact with the outside environment, blood groups, etc.

64
Q

What makes different isomers?

A

the distribution of hydroxyl and charge groups

65
Q

What are oligosaccharides important for?

A

structure, energy storage, and molecule signaling// defines blood type

66
Q

How is mobility limited in a polysaccharide?

A

tail to tail interactions limit mobility, and allow mobility

67
Q

What is a macromolecule?

A

polymer formed from monomers or subunits that are linked together through covalent bonding

68
Q

What does a double bond in the tail of a triglyceride mean?

A

that it’s unsaturated

69
Q

How are bilayer membranes possible?

A

When there is a bubble of hydrophobic tails

70
Q

Isoprenes form what basic subunit that forms the backbone of cholesterol?

A

isoprenoids

71
Q

Why don’t cholesterol molecules spin?

A

they’re shape is extremely planar

72
Q

Are glycolipids phospholipids? Why or why not?

A

They are not because they don’t have phosphate groups

73
Q

What is the formula for amino acids?

A

Carbon, amino group, carboxyl group, r side group chain

74
Q

What kind of isomers are proteins formed through?

A

L isomers

75
Q

Does electron density restrict rotation?

A

Yes

76
Q

What are the pyrimidines?

A

uracil (only found in RNA), cytosine, and thymine

77
Q

What are the purines?

A

adenine and guanine

78
Q

What part of the base-sugar linkage distinguishes DNA from RNA?

A

the 2’ carbon

79
Q

What kind of proteins control where and when certain proteins are expressed?

A

receptor proteins

80
Q

What will depolymerize a microtubule?

A

extreme cold

81
Q

What are the two most common properties of protein folding?

A

alpha helix and beta pleated sheets

82
Q

Is a proteins function disrupted if it’s not folded correctly?

A

Yes

83
Q

What can abnormal folding lead to?

A

extreme conditions and disease states

84
Q

What does every protein have?

A

amino terminal and carboxy terminal

85
Q

Can you denature and renature (unfold and refold) in certain environments?

A

yes

86
Q

Primary structure

A

amino acid sequence

87
Q

Secondary structure

A

charge charge interaction, R group interactions

88
Q

tertiary structure

A

water contributes to this structure

89
Q

What gives a protein its shape?

A

R group interactions

90
Q

Low energy equals…

A

less flexibility

91
Q

Does the R group side chain also determine properties of the proteins along with shape?

A

yes

92
Q

what kinds of disorders have been linked to the misfolding of proteins?

A

neurodegenerative disorders/ alzheimers, dementia, etc

93
Q

A cell experiences more dysfunction when…

A

the aggregates get bigger

94
Q

What do lysozymes do?

A

breakdown carbohydrates

95
Q

What are 80% of medications?

A

natural products such as plants, microbes, etc

96
Q

can you have multiple domains within the same protein? if yes can they perform different things?

A

yes, they can perform different things

97
Q

hemoglobin has 4 subunits to the molecule, what are they?

A

2 alpha helixes and 2 beta pleated sheets

98
Q

what is a homodimer?

A

2 proteins interacting with a single identical binding site

99
Q

what is a homotetramer?

A

4 different subunits acting at different sights

100
Q

is every subunit composed of the same number of amino acid sequences?

A

yes

101
Q

explain the structural reasons for sickle cell anemia.

A

a single amino acid difference alters the structure to where it is still functional, however leads to a shape change of the red blood cell

102
Q

is tubulin a heterodimer or a homodimer?

A

heterodimer

103
Q

since elastin isn’t very rigid and can react, what does it allow?

A

it allows the tissue to stretch

104
Q

After elastin stretches it…

A

goes back to same structure just with different folding patterns

105
Q

are all r groups charged at active sites?

A

yes, allows them to have interactive capabilities

106
Q

What happens when an antigen binding site is hit?

A

it starts making as many antibodies as they can as quick as they can

107
Q

What happens when a substrate gets into enzyme state?

A

lowers the activation energy

108
Q

What do hydrolysis reactions do?

A

break down molecules

109
Q

Why do we prefer to use organic and natural things for modern medicine?

A

It is easier for us to deduce and synthesize ourselves

110
Q

How do cells obtain energy through respiration?

A

they obtain energy by the oxidation of organic molecules

111
Q

What do photosynthetic organisms use to synthesize organic molecules?

A

sunlight

112
Q

What subunits do cells obtain most of their energy from?

A

mitochondria and chloroplast inner membranes

113
Q

water is the original electron donor in…

A

photosynthesis

114
Q

oxygen is the final electron acceptor in…

A

respiration

115
Q

What generates ATP from ADP & phosphate?

A

the flow of hydrogen and protons through an ATP-synthase enzyme

116
Q

What features do mitochondria and chloroplasts share?

A

contain own DNA & ribosomes, translate some of their own proteins, inner membranes contain protein complexes for ATP synthesis

117
Q

In what way do chemical reactions proceed?

A

in the direction that causes a loss of free energy

118
Q

Do all reactions, cellular or not, require activation energy to get them started?

A

yes

119
Q

What do enzymes do?

A

convert substrates into products while remaining unchanged themselves

120
Q

Are enzymes consumed during reactions?

A

no

121
Q

Enzyme catalyzed reactions depend on…

A

rapid molecular collisions

122
Q

What kind of interactions allow enzymes to bind specific molecules at the enzyme active site?

A

non covalent interactions

123
Q

What is the most used activated carrier?

A

ATP

124
Q

what is the only way to get rid of a covalent linkage?

A

breaking those covalent bonds

125
Q

tyrosine phosphorylation is very closely related to…

A

cell growth, cell multiplication, cancer, etc

126
Q

name the enzyme that can take away phosphate groups.

A

phosphatase

127
Q

what are the 2 groups of protein kinases?

A

tyrosine & serine/threonine

128
Q

what do G proteins do?

A

they regulate and signal the cells

129
Q

what subunit allows GDP to bind to it?

A

the alpha subunit

130
Q

describe scaffolds

A

structures that can serve as binding sites to recruit some interacting proteins depending on their functions

131
Q

Are scaffold proteins membrane bound?

A

no, they are transient proteins

132
Q

Are scaffold proteins membrane bound?

A

no, they are transient proteins

133
Q

when does phase transition occur?

A

from protein protein interactions

Cell Biology (4 decks)

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