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Cellular Biology (BIOL2020) > Midterm 1 > Flashcards

Midterm 1 Flashcards

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1
Q

What are proteins made of?

A

Amino Acids

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2
Q

What are nucleic acids made of?

A

Nucleotides

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3
Q

What are polysaccharides made of?

A

Carbohydrates

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4
Q

What are lipids made of?

A

Fatty acids

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5
Q

What are the four main types of macromolecules?

A

Proteins, Nucleic Acids, Polysaccharides, and Lipids

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6
Q

All macromolecules are built from monomers except for?

A

Lipids

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7
Q

What is an oligosaccharide?

A

A small chain of monosaccharides?

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8
Q

What is a fat made of?

A

A fat is a triglycerol: made of 3 fatty acid tails, and one glycerol

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9
Q

What is the difference between a phospholipid and a fat?

A

Phospholipids have 2 fatty acid tails and fats have 3 fatty acid tails.

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10
Q

A fatty acid is composed of….

A

Hydrocarbon chains (hydrophobic) and a carboxyl group (hydrophilic)

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11
Q

Fats, steroids, and phospholipids are all examples of…

A

Lipids

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12
Q

Describe the structure of a steroid

A

4 hydrocarbon rings with a hydroxyl group attached to one of the rings

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13
Q

What are the 3 types of proteins?

A

Enzymes, structural, and regulatory

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14
Q

How do amino acids hook together?

A

Peptide bonds

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15
Q

What is an amino acid formed of?

A

An amino group, alpha carbon, hydrogen ion, carboxyl group and a side chain (R group)

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16
Q

What gives an amino acid its determining characteristics?

A

The R group

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17
Q

What is a peptide?

A

A short chain of amino acids

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18
Q

What is a protein?

A

A folded polypeptide

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19
Q

Describe the four levels of structures

A

1) Primary: linear strain
2) Secondary: alpha helix
3) Tertiary: folded alpha helices
4) Quaternary: group of tertiary structures

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20
Q

What is the function of Ribonuclease A?

A

Digest RNA

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21
Q

What is a molecular chaperone?

A

A protein that binds to another to protect it by changing it’s shape

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22
Q

Why are cells compartmentalized?

A

Separate functions, prevents random movement through membrane, protect from outer activities

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23
Q

What are some membrane functions?

A

Provide selective barrier, help with cell to cell interactions

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24
Q

What are membranes composed of?

A

Lipids, Carbs, Proteins

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25
Q

_____ makes up most of membrane lipids

A

Phospholipids

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26
Q

Up to __% of the membrane can be composed of cholesterol.

A

50

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27
Q

Lipids are easily able to switch places side by side but in order to flip they require help from membrane proteins containing _____.

A

Flippase

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28
Q

Why do holes in the lipid bilayer seal almost immediately?

A

Because hydrophobic tails become exposed so lipids move together to prevent water touching the tails

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29
Q

How do carbs attach to the membrane?

A

Binding covalently to lipids or proteins

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30
Q

All carbs are either ___ or ___ linked

A

Nitrogen, Oxygen

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31
Q

Carbs never face ___ the cytoplasm

A

Into

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32
Q

What does asymmetric mean in terms of the membrane?

A

Something can be attached to one side of the membrane but not the other

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33
Q

What is the difference between integral and peripheral proteins?

A

Integral proteins are embedded in the membrane, and peripheral are blinded to the outside/inside layer of the membrane

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34
Q

How are peripheral proteins attached to the membrane?

A

to integral proteins via electrostatic bonds

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35
Q

What is a GPI anchored protein?

A

A protein that is bound to a lipid

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36
Q

What are the four features of the fluid mosaic model?

A

asymmetric, embedded, mosaic, and quasifluid

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37
Q

What are the 3 types of membrane lipids?

A

Glycolipids, Phospholipids and Cholesterol

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38
Q

Are peripheral proteins hydrophilic, hydrophobic or amphipathic?

A

Hydrophilic

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39
Q

What is a sphingolipid?

A

Long chain hydrocarbons come together in membrane, pack tightly and become gel like, like a lipid raft

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40
Q

What is a lipid raft?

A

Tightly packed lipids/cholesterol in a patch on the membrane outer leaflet where GTI proteins can attach

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41
Q

The ____ is central to the microtubules

A

Mitochondria

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42
Q

What is metabolism?

A

collection of all biochemical reactions

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43
Q

The ___ pathway takes complex structures and breaks them into smaller components so the molecules can be reused. Produces energy

A

Catabolic

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44
Q

The _____ pathway takes simple components and builds more complex ones by using energy

A

Anabolic

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45
Q

What are a few functions of the mitochondria?

A

Synthesizing amino acids, calcium transport

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46
Q

What is the function of Drp1

A

binds/hydrolyzes GTP, involved in splitting mitochondria in half

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47
Q

What is the crust and where is it located?

A

in the inner membrane, increases SA

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48
Q

What is the inter membrane?

A

located between the inner and outer membrane

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49
Q

What is a porin?

A

A major protein channel in the mitochondrial membrane allowing ATP transfer when open. Located in outer mitochondrial membrane

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50
Q

Does the inner membrane contain more protein or more lipids?

A

3-4 protein: 1 lipid

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51
Q

___ is the loss of electrons and ___ is the gain of electrons

A

oxidation, reduction

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52
Q

What is glycolysis?

A

the pathway of glucose oxidation

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53
Q

What is produced by glycolysis?

A

pyruvate, 2 ATP, 2 NADH

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54
Q

NADH accepts _ é and _ H+

A

2, 1

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55
Q

What is NADH?

A

A co-factor

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56
Q

Pyretic Acid + Co A + NAD ->

A

Co A + 2 C chain + NADH + CO2

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57
Q

What is pyruvate broken down into?

A

acetyl group, 2e, 2 H+, CO2

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58
Q

What do you get as products in the TCA cycle?

A

CO2, NADH, FADH2, GTP, Oxaloacetic acid

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59
Q

Cells cannot use electrons as energy, it must be converted into ?

A

ATP

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60
Q

____ reacts with acetyl Co A to start the TCA cycle again

A

Oxaloacetic acid

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61
Q

How many times does the TCA cycle occur for every molecule of glucose?

A

2

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62
Q

What is oxidative phosphorylation?

A

The formation of ATP driven by the transfer of é to oxygen

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63
Q

What is the electrochemical gradient?

A

change in voltage/concentration across the membrane

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64
Q

What is chemiosmosis?

A

the production of ATP using the energy of H+ gradients across membrane to phosphorylate ADP

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65
Q

2,4-dinitrophenol inhibits chemiosmosis by?

A

Uncoupling é transport and ATP synthesis

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66
Q

What are the four main organelles that are part of the endomembrane system?

A

Golgi, ER, Endo/Lysosomes

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67
Q

What is the function of the endomembrane system?

A

Involved in synthesizing membranes and moving stuff around

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68
Q

Which side of the ER membrane contains ribosomes?

A

Cytosolic side

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69
Q

What are the functions of the sER?

A

Synthesis of steroid hormones, detoxification, and sequestering calcium

70
Q

Where are the proteins synthesized?

A

Ribosomes

71
Q

What is cell fractionation?

A

A technique used to show that free ribosomes make different kinds of proteins than membrane bound ribosomes

72
Q

What experiment was used to examine the secretion pathway?

A

Pulse Chase Experiment

73
Q

What is a yeast sec mutant?

A

yeast with degenerative genes which synthesize secretory proteins but won’t secrete the proteins

74
Q

Yeast sec will secrete proteins at room temp but will stop secreting proteins when the temp is ____.

A

increased

75
Q

What happens when mRNA is translated?

A

protein is created

76
Q

Proteins can accumulate in which 5 places which can block the secretion pathway?

A

2x Vesicles, Cytosol, ER, Golgi

77
Q

What does a signal recognition particle do?

A

binds to signal sequence on ribosome causing translation to stop and elongation of polypeptide to occur

78
Q

How does the cell know if a protein should be inserted into the membrane?

A

Amino end of protein has signal sequence telling it would be inserted into the membrane

79
Q

What side of the ER membrane has the signal sequence receptor on it?

A

Cytosolic side

80
Q

What is a translocon?

A

a group of integral membrane proteins and SPP complex that forms a channel

81
Q

How does con translational translocation mechanism work?

A

Protein is synthesized by hydrophobic amino acids as it goes through the membrane. Stop sequence forms, hydrophobic part secreted into membrane

82
Q

What are the names of the 2 leaflets of membrane?

A

cytosolic, exoplasmic

83
Q

Why are lipids difficult to synthesize in the cytosol?

A

because of the hydrophobic tails

84
Q

What is the function of flippase?

A

flippase flips lipids from one leaflet of membrane to the other because integral membrane proteins only produce lipids into one leaflet of the membrane so in order for both layers to grow, the material from one leaflet must be flipped to the other side

85
Q

How are lipids transferred through the cell?

A

Proteins bin to them covering hydrophobic bits

86
Q

What is an O-linked protein?

A

A protein that attaches to serine/theronine

87
Q

What is an N-linked protein?

A

a protein that attaches to asparagine

88
Q

Where does O-linkage occur?

A

Golgi

89
Q

Where does N-linkage occur?

A

ER/Golgi/ERGIC

90
Q

What is the function of Dolichol Phosphate?

A

moves sugar around membrane

91
Q

How many sugars can a dolichol carry at once?

A

7

92
Q

What does oligosaccharyltransferase do?

A

transfers sugar/dolichol chain into an asparagine covalent linkage

93
Q

What is the point of quality control?

A

allows cell to select/destroy misfiled protein

94
Q

What are the names of the 2 ER proteins responsible for quality control?

A

Calnexin and Calreticium

95
Q

What is the function of calnexin?

A

Cuts off glucose and tries to fold it correctly

96
Q

What is the function of calreticium?

A

binds to protein by glucose, cuts glucose off and protein is released

97
Q

What does the enzyme UGGT do?

A

detects if proteins are folded correctly by checking if hydrophobic regions are exposed to lumen. Then it cuts off the mannose of proteins until it can no longer fold and a proteasome will destroy it.

98
Q

What is the function of a proteasome?

A

protein machine that destroys other proteins

99
Q

What are proteolytic enzymes?

A

enzymes that destroy proteins

100
Q

What is ubiquitin?

A

a signal for the protein to be destroyed, threads protein into proteasome channel

101
Q

What attaches ubiquity to the protein?

A

ubiquitin ligase

102
Q

What happens to a cell containing too many misfiled proteins?

A

It will die (apoptosis)

103
Q

What is the function BiP?

A

Once cell realizes a protein is misfiled. BiP tries to refold the protein

104
Q

What is the function of the translation factor ELF2 Alpha?

A

turns of protein translation so bad proteins aren’t made

105
Q

What is apoptosis?

A

programmed cell death

106
Q

What is the endoplasmic reticulum Golgi Intermediate Compartment(ERGIC)?

A

Space between the ER/Golgi

107
Q

What are 3 regions of the Golgi complex called?

A

cis/medial/trans cisternae

108
Q

The __ cistern is closest to the ER while the __ cisternal is closest to the plasma membrane.

A

Cis, Trans

109
Q

Where are proteins usually modified?

A

Golgi, Integral Membrane Proteins

110
Q

What are the 2 ways that stuff moves through the Golgi?

A

Vesicular transport, Cisternal Maturation model

111
Q

What is the difference between vesicular transport and the cisternal maturation model?

A

CMM: retrograde, no vesicles
VT: vesicles, anterograde

112
Q

How do vesicles break off of the organelle?

A

protein on surface coating of vesicles forces membrane to curve which causes the vesicle to snap off of the organelle.

113
Q

What do COP2 coated vesicles do?

A

Move via anterograde to ERGIC/Golgi from ER or form cis to trans

114
Q

What do COP1 coated vesicles do?

A

Move via retrograde from ERGIC/Golgi to ER or from trans to cis

115
Q

What do clathrin coated vesicles do?

A

Move from trans Golgi network to endo/lysosomes and from PM to cytoplasmic compartments

116
Q

How are ER proteins secreted?

A

Vesicles bud off of ER

117
Q

What are the functions of a coated vesicle?

A

help shape vesicle, help select which proteins need to be moved

118
Q

What does Sar1 do?

A

regulatory protein, responsible for formation of COP2 vesicles

119
Q

How does COP2 get rid of its coat?

A

when the vesicle finds its desired location, GTP is hydrolyzed to GDP making the coat fall off

120
Q

What is retention?

A

“if a protein is supposed to be in the ER than it stays in the ER” keeping what is meant to stay

121
Q

What does ARF1 do?

A

regulatory protein responsible for formation of COP1 vesicles

122
Q

What is retrieval?

A

retrieving a vesicle that took the wrong proteins to the wrong place, COP1 takes them back

123
Q

What kind of protein recognizes if there is an incorrect protein in a vesicle?

A

Transmembrane proteins

124
Q

What is the KDEL sequence at the end of a protein?

A

Lys-asp-glu-leu

125
Q

What is the function of a lysosome?

A

destroys parts of cell that are no longer needed

126
Q

How many enzymes do lysosomes contain?

A

50 works best in low pH

127
Q

How do enzymes not destroy the lysosome?

A

lumen inside of membrane is very glycosylated which protects the membrane

128
Q

How do lysosomes know when to destroy cell part?

A

Autophagosome surrounds organelle, lysosome binds to autophagosome and destroys the organelle

129
Q

How are lysosomal enzymes taken to the lysosome?

A

coated vesicles from ER take them there

130
Q

How do particles in vesicle get to target membrane?

A

vesicle membrane bind

131
Q

What is tethering?

A

fibrous proteins tether vesicle to target

132
Q

What do rabs do?

A

bind to GTP, help with tethering

133
Q

What is docking?

A

fibrous proteins pull vesicle tighter and eventually fuse

134
Q

The proteins on membrane and vesicles that determine where they go are called?

A

t/v-SNAREs

135
Q

What are the 2 types of t SNAREs

A

syntaxin, SNAP 25

136
Q

What is the name of a v-SNARE

A

synaptobrevin

137
Q

What do SNAREs do?

A

bring vesicle closer to membrane via helical complex

138
Q

What is the function of the NSF?

A

binds to SNARE complex and break it apart allowing t/v membranes to form together making a pore

139
Q

What is a ligand?

A

anything taken into cell by endocytosis

140
Q

There is a concentration of _____ that forms on a coated pit

A

LDL: Low density lipoprotein cholesterol

141
Q

Describe the composition of clathrin?

A

3 heavy chains, 3 light chains, in Triskelion shape

142
Q

The cytosolic membrane of a vesicle has one layer of ___ and one layer of ___ ___

A

clathrin, adapter proteins

143
Q

What kind of structure does an adapter protein have?

A

quaternary

144
Q

What is GTPyS

A

a kind of nonhydrolyzable GTP

145
Q

What does Dynamin do?

A

hydrolyzes GTP causing conformational change in neck region of clathrin

146
Q

What do house keeping receptors do?

A

bind to things cell needs

147
Q

What do signalling receptors do?

A

bind to info containing molecules

148
Q

What is endocytosis?

A

movement from outside cell to inside cell

149
Q

Why would a cell want to degrade signal proteins?

A

to prevent over stimulation

150
Q

Where does postranslational uptake of proteins occur?

A

nucleus, mitochondria, peroxisomes, and chloroplast

151
Q

Name the 4 mitochondrial compartments?

A

Inner/outer membane, Inter membrane space, matrix

152
Q

What is required to transfer a protein into mitochondria?

A

a transfer sequence telling the mitochondria to take in the protein

153
Q

Describe the function of chaperone proteins?

A

affect the folding of other proteins, no structural info, recognize unfolded proteins, help them find their tertiary structure, require energy

154
Q

Why are mitochondrial DNA synthesized in the nucleus?

A

Because they have encoded DNA

155
Q

The ___ doesn’t make any mitochondrial proteins so it gets its proteins from the _____

A

mitochondria, nucleus

156
Q

Hsp 60 and Hsp 70 are examples of….

A

Chaperone proteins

157
Q

Hsp 7 interacts with proteins made in ____ to assist in _____

A

cytosol, folding

158
Q

What makes protein unfold in the matrix?

A

Hsp60/70, requires energy, chaperone hydrolyzes ATP, folds protein, pulls into matrix

159
Q

What are amino acids made of?

A

A carboxyl group, amino group and side (r) chain

160
Q

Carbs only attach to the _____ leaflet

A

exoplasmic

161
Q

What kind of proteins are Myristate and Farnesyl?

A

GPI anchored proteins

162
Q

____ is involved in membrane fluidity

A

Cholesterol

163
Q

___ _____ move as a unit

A

Lipid rafts

164
Q

Where are F1 particles located?

A

the inner mitochondrial membrane

165
Q

Where does glycolysis take place?

A

The mitochondria/cytosol?

166
Q

What is the purpose of the proton motive force in the case of this class?

A

Drives synthesis of ATP by chemiosmosis

167
Q

What is 2,4-dinitophenol?

A

Passage ways in membrane for H+ to travel across

168
Q

What does the F1 Complex (ATPsynthase) do?

A

changes ATP to ADP + Pi

169
Q

Which unit of the binding change mechanism is the rotating unit?

A

Gamma

170
Q

The beta subunits of the binding change mechanism are always in different conformations which are:

A

tight, loose, open

171
Q

Microbodies, Peroxisomes, Glyoxysomes are all similar to…

A

the mitochondria

Cellular Biology (BIOL2020) (3 decks)

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