Final Flashcards

(164 cards)

1
Q

prokaryotic cell

A
  • cell wall
  • nucleoid + single/looped chromosome
  • no membrane bound organelles
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2
Q

eukaryotic cell

A
  • no cell wall
  • membrane bound organelles
  • nucleus + multiple chromosomes
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3
Q

plasma membrane

A
  • bilayer of lipid molecules (with hydrophobic heads + hydrophilic tails) that form the cellular membrane
  • provides structure
  • regulates entry and exit of molecules into and out of the cell
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4
Q

cytoskeleton

A
  • provides cellular structure
  • facilitates movement of cell + transport of molecules within the cell
  • allows for localization of biochemical activities
  • composed of microtubules, microfilaments, and intermediate filaments
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5
Q

microfilaments (actin filaments)

A
  • solid rods made of actin found in the cytoplasm of the cell
  • facilitate cell movement
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6
Q

microtubules

A
  • hollow rods composed of tubulin
  • facilitate cell division
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7
Q

intermediate filaments

A
  • more stable than other cytoskeleton subunits
  • confer stability + structural support for a cell
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8
Q

nucleus (structure)

A
  • double membrane bound organelle
  • nuclear envelope regulates nuclear entry
  • contains nucleolus
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9
Q

DNA-containing organelle

A

nucleus

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10
Q

site of DNA replication

A

nucleus

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11
Q

organelle in which ribosome assembly begins

A

nucleolus

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12
Q

rough ER (structure)

A
  • series of invaginated membranes (large surface area)
  • ribosomes attached
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13
Q

site of protein synthesis

A

ribosomes (on rough ER)

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14
Q

modification of newly made proteins

A

rough ER (lumen)

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15
Q

origin site of transport vesicles (transport vesicles bud off ___)

A

rough ER

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16
Q

smooth ER (structure)

A
  • series of invaginated membranes (large surface area)
  • no attached
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17
Q

smooth ER (structure)

A
  • series of invaginated membranes (large surface area)
  • no attached ribosomes
  • more tubular than rough ER
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18
Q

organelle which chemically modifies small molecules

A

smooth ER

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19
Q

organelle responsible for hydrolysis of glycogen

A

smooth ER

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20
Q

organelle which synthesizes lipids & steroids

A

smooth ER

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21
Q

golgi complex (structure)

A
  • series of small, flattened sacs & membrane-bound vesicles
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22
Q

organelle resposible for concentration, packaging, and sorting proteins

A

golgi complex

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23
Q

organelle which modifies proteins received from rough ER

A

golgi complex

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24
Q

organelle which synthesizes polysaccharides for plant cell wall

A

golgi complex

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25
mitochondrion (structure)
- double-membrane bound - matrix formed by inner membrane; contains ribosomes, DNA, and enzymes used for energy conversion
26
organelle responsible for generating most cellular energy
mitochondria
27
location of energy generation in mitochondria
mitochondrial matrix
28
cellular locations of ribosomes
- free in cytoplasm - attached to rough ER - in mitochondria + chloroplasts
29
ribosome (structure)
- ribosomal RNA (rRNA) + protein molecules
30
primary lysosomes are generated by the ______
golgi complex
31
purpose of primary lysosomes
- contain digestive enzymes - can fuse with phagosomes/endosomes to form secondary vesicles
32
secondary vesicles are formed via ______
fusion of primary vesicles + phagosomes/endosomes
33
purpose of secondary lysosomes
- break down molecules & release material from cells
34
secretory pathway
1. proteins synthesized in ribosomes of rough ER 2. transport vesicle carries proteins from rough ER to golgi complex for modification & packaging 3. secretory vesicles bud off golgi complex 4. secretory vesicle fuses with plasma membrane & contents are released to extracellular space (exocytosis)
35
endocytosis
- uptake of molecules into the cell via endosomes - small molecules
36
phagocytosis
- uptake of molecules into the cell via phagosomes - large molecules (food, bacteria, etc)
37
turnover
- continuous breakdown of proteins & other cellular components in a cell - allows molecules to be reused to make new proteins, etc
38
autophagy
- lysosome digestion of a cell's own components/materials (organelles, etc) - allows materials to be reused
39
covalent bond
- sharing of electron pairs between molecules - can be polar or nonpolar
40
type of bond: C--C
nonpolar covalent
41
type of bond: O--O
nonpolar covalent
42
type of bond: C--O
polar covalent
43
ionic bond
- attraction resulting from distinct, differing electrical charges on atoms
44
type of bond: Na--Cl
ionic
45
hydrogen bond
bond between hydrogen atom + electronegative atom
46
type of bond: H--O
hydrogen
47
type of bond: H--N
hydrogen
48
hydrophobic interactions
- tendency of nonpolar compounds to group together in an aqueous environment - spontaneous (increases entropy)
49
van der Waal's forces
- temporary attractions between molecules - results from movement of electrons in cloud around atom - allows for interactions between nonpolar/uncharged molecules (ex. carbon atoms with fully occupied orbitals
50
dissociation constant (Ka)
- quantifies the ability of an acid to dissociate in water, as weak acids are more likely to exist as contiguous molecules in water, while strong acids are more likely to dissociate
51
high Ka indicates a ____ acid
strong (more dissociation)
52
low Ka indicates a _____ acid
weak (less dissociation)
53
pKa
pH at which an acid is half-dissociated
54
Zwitterionic form
- amino acid form in which the carboxyl group is deprotonated and the amino group is protonated - state in which amino acids are typically found at neutral pH
55
alanine side chain properties
nonpolar/hydrophobic
56
alanine functional group
"simple" aliphatic (CH3)
57
glycine side chain properties
nonpolar/hydrophobic
58
glycine functional group
"simple" aliphatic (H)
59
phenylalanine side chain properties
nonpolar/hydrophobic
60
phenylalanine functional group
aromatic
61
leucine side chain properties
nonpolar/hydrophobic
62
leucine functional group
aliphatic
63
isoleucine side chain properties
nonpolar/hydrophobic
64
isoleucine functional group
aliphatic
65
histidine side chain properties
- positive/hydrophilic - can be positive or neutral at physiological pH
66
histidine functional group
imidazole ring
67
cysteine side chain properties
- polar - terminal sulfur + able to form disulfide bridges with other cysteines
68
cysteine functional group
sulfhydryl
69
proline side chain properties
- nonpolar/hydrophobic - capable of self-bonding (bond forms between side chain and amino group)
70
proline functional group
weird aliphatic (self-bonding creates a ring)
71
methionine side chain properties
nonpolar/hydrophobic
72
methionine functional group
aliphatic
73
first amino acid in all polypeptides
methionine
74
glutamate side chain properties
negative
75
glutamate functional group
carboxylic acid
76
aspartate side chain properties
negative
77
aspartate functional group
carboxylic acid
78
glutamine side chain properties
polar
79
glutamine functional group
carboxyamide
80
asparagine side chain properties
polar
81
asparagine functional group
carboxyamide
82
valine side chain properties
nonpolar/hydrophobic
83
valine functional group
aliphatic
84
tryptophan side chain properties
nonpolar/hydrophobic
85
tryptophan functional group
aromatic
86
serine side chain properties
polar
87
serine functional group
hydroxyl
88
threonine side chain properties
polar
89
threonine functional group
hydroxyl
90
tyrosine side chain properties
polar
91
tyrosine functional group
hydroxyl
92
lysine side chain properties
positive/hydrophilic
93
lysine functional group
amino
94
arginine side chain properties
positive/hydrophilic
95
arginine functional group
guanidinium
96
bonds in a polypeptide around which rotation can occur
phi & psi bonds
97
bond in a polypeptide around which rotation cannot occur
peptide bond
98
primary structure
a protein's amino acid sequence
99
secondary structure
alpha helices & beta pleated sheets
100
pattern of hydrogen bonding in alpha helices
hydrogen bond occurs between carbonyl of amino acid i and i+4
101
pattern of hydrogen bonding in beta pleated sheets
- sheets stabilized by hydrogen bonding between 2-antiparallel beta strands - each amino acid forms 2 hydrogen bonds
102
tertiary structure
- protein folding into 3D conformation - driver by weak interactions
103
quaternary structure
interactions between multiple polypeptides to form complex proteins
104
orientation of bonds in parallel beta sheets
- amino acid 1 bonds 2x to 2 other amino acids - forms 2x hydrogen bonds (one each)
105
orientation of bonds in anti-parallel beta sheets
- amino acid 1 bonds 2x to 1 other amino acid - it's the like more even one but it's antiparallel
106
tertiary structure of myoglobins
- myoglobins primarily in aqueous environment - hydrophobic amino acids oriented towards interior; hydrophilic on outside
107
tertiary structure of porins
- porins often embedded in membranes (hydrophobic environment) - hydrophobic amino acids oriented towards outside (interacting with environment); hydrophilic amino acids on interior - "inside-out" orientation
108
hemoglobin quaternary structure
- 2 alpha globins + 2 beta globins = 4 linked polypeptides - heterotetramer (four non-identical amino acids)
109
3 major differences between DNA & RNA
- DNA = double helix; RNA = single-stranded - DNA ribose = no hydroxyl on 2' carbon; RNA = additional hydroxyl group - DNA = thymine; RNA = uracil
110
nucleoside
- 5 carbon sugar + nitrogenous base - nucleotide without phosphate group(s)
111
location of phosphodiester bond in nucleotides
5'C
112
location of betaglycosidic linkage in nucleotides
1'C
113
locations of bonds joining chains of nucleotides
3'OH - oxygen - phosphate - oxygen - 5'C
114
chemical basis for stem-loop structures in RNA
possible because RNA is single-stranded; does not form double helix/complementary base pairs (no complementary strand -> stem loop & non-Watson-Crick base pairing possible)
115
in DNA, antiparallel conformation facilitates _____
hydrogen bonding
116
A-T base pairs form ___ hydrogen bonds
2
117
C-G base pairs form ___ hydrogen bonds
3
118
two types of chemical interactions which strengthen DNA molecules
- hydrogen bonding (between base pairs) - van der Waal's interactions (between "stacked" pairs)
119
"lock and key" model of enzyme-substrate interaction
theory that enzymes naturally fit into active sites & enzyme conformation does not change
120
induced-fit model of enzyme-substrate interaction
theory that bond with enzyme induces conformational change in enzyme which facilitates substrate binding
121
4 types of interactions that can be occur between an enzyme & substrate in enzyme active site
- hydrogen bonding - van der Waal's - ionic interactions - hydrophobic interactions
122
competitive inhibition ____ Vmax
does not affect
123
competitive inhibition ____ Km
increases
124
uncompetitive inhibition ____ Vmax
decreases
125
uncompetitive inhibition ____ Km
decreases
126
noncompetitive inhibition ____ Vmax
decreases
127
noncompetitive inhibition ____ Km
does not affect
128
3 fractions produced in cell fractionation by differential centrifugation
- nuclear - mitochondrial - microsomal
129
gel filtration chromatography
separates proteins according to size
130
ion-exchange chromatography
separates proteins according to ionic charge
131
affinity chromatography
isolates proteins via binding of a protein to a ligand capable of specific binding
132
immunoprecipitation
used to isolate proteins
133
co-immunoprecipitation
used to identify molecules which interact with protein of interest in the cell
134
monoclonal antibody
- identical copies of antibody - can bind antigen on one epitope (one antibody per antigen)
135
polyclonal antibodies
- antibodies capable of binding same antigen on different epitopes - can bind multiple antibodies per antigen
136
sucrose bonds via a _____ glycosidic linkage
1,2
137
lactose bonds via a _____ glycosidic linkage
1,4
138
maltose bonds via a _____ glycosidic linkage
1,4
139
bonds in cellulose indigestible by humans
beta-1,4
140
____ is the major phospholipid from which most membrane phospholipids are derived
phosphatidate
141
pepsin inactive form
pepsinogen
142
pepsinogen activated by ____
- HCl (partially activated) - pepsinogen - pepsin
143
cholecystokinin (CCK)
- digestive hormone - signals pancreas to release digestive enzymes - signals gallbladder to release bile salts
144
secretin
- digestive hormone - induces pancreas to release sodium bicarbonate
145
trypsin zymogen
trypsinogen
146
trypsin activated by ____
- trypsin - enteropeptidase
147
chymotrypsin zymogen
chymotrypsinogen
148
chymotrypsin activated by ____
trypsin
149
carboxypeptidase zymogen
procarboxypeptidase
150
carboxypeptidase activated by ____
trypsin
151
lipase zymogen
prolipase
152
lipase activated by
trypsin
153
alpha-amylase cleaves
alpha-1,4 bonds
154
alpha-glucosidase cleaves
alpha-1,4 bonds
155
maltase cleaves
alpha-1,4 bonds
156
dextrinase cleaves
alpha-1,6 bonds
157
maltase cleaves ____ to _____
- maltose - 2 molecules glucose
158
sucrase cleaves ____ to _____
- sucrose - glucose + fructose
159
lactase cleaves ____ to _____
- lactose - glucose and galactose
160
glucose and galactose are taken up into intestinal cells via _____, a form of active transport
the SGLT - sodium-linked glucose transporter
161
fructose is taken up into intestinal cells via the ____
GLUT5 transporter
162
glucose, fructose, and galactose are transported out of the cell via the ____
GLUT2 transporter
163
CCK behavioral effects
- increased satiety - decreased food intake - decreased body weight
164
NAD+ is _____; NADH is _____
oxidized; reduced