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BIOL 100 > Final > Flashcards

Final Flashcards

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
Q

mitochondrion (structure)

A
  • double-membrane bound
  • matrix formed by inner membrane; contains ribosomes, DNA, and enzymes used for energy conversion
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26
Q

organelle responsible for generating most cellular energy

A

mitochondria

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27
Q

location of energy generation in mitochondria

A

mitochondrial matrix

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28
Q

cellular locations of ribosomes

A
  • free in cytoplasm
  • attached to rough ER
  • in mitochondria + chloroplasts
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29
Q

ribosome (structure)

A
  • ribosomal RNA (rRNA) + protein molecules
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30
Q

primary lysosomes are generated by the ______

A

golgi complex

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31
Q

purpose of primary lysosomes

A
  • contain digestive enzymes
  • can fuse with phagosomes/endosomes to form secondary vesicles
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32
Q

secondary vesicles are formed via ______

A

fusion of primary vesicles + phagosomes/endosomes

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33
Q

purpose of secondary lysosomes

A
  • break down molecules & release material from cells
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34
Q

secretory pathway

A
  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)
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35
Q

endocytosis

A
  • uptake of molecules into the cell via endosomes
  • small molecules
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36
Q

phagocytosis

A
  • uptake of molecules into the cell via phagosomes
  • large molecules (food, bacteria, etc)
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37
Q

turnover

A
  • continuous breakdown of proteins & other cellular components in a cell
  • allows molecules to be reused to make new proteins, etc
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38
Q

autophagy

A
  • lysosome digestion of a cell’s own components/materials
    (organelles, etc)
  • allows materials to be reused
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39
Q

covalent bond

A
  • sharing of electron pairs between molecules
  • can be polar or nonpolar
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40
Q

type of bond: C–C

A

nonpolar covalent

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41
Q

type of bond: O–O

A

nonpolar covalent

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42
Q

type of bond: C–O

A

polar covalent

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43
Q

ionic bond

A
  • attraction resulting from distinct, differing electrical charges on atoms
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44
Q

type of bond: Na–Cl

A

ionic

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45
Q

hydrogen bond

A

bond between hydrogen atom + electronegative atom

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46
Q

type of bond: H–O

A

hydrogen

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47
Q

type of bond: H–N

A

hydrogen

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48
Q

hydrophobic interactions

A
  • tendency of nonpolar compounds to group together in an aqueous environment
  • spontaneous (increases entropy)
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49
Q

van der Waal’s forces

A
  • 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
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50
Q

dissociation constant (Ka)

A
  • 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
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51
Q

high Ka indicates a ____ acid

A

strong (more dissociation)

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52
Q

low Ka indicates a _____ acid

A

weak (less dissociation)

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53
Q

pKa

A

pH at which an acid is half-dissociated

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54
Q

Zwitterionic form

A
  • 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
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55
Q

alanine side chain properties

A

nonpolar/hydrophobic

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56
Q

alanine functional group

A

“simple” aliphatic (CH3)

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57
Q

glycine side chain properties

A

nonpolar/hydrophobic

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58
Q

glycine functional group

A

“simple” aliphatic (H)

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59
Q

phenylalanine side chain properties

A

nonpolar/hydrophobic

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60
Q

phenylalanine functional group

A

aromatic

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61
Q

leucine side chain properties

A

nonpolar/hydrophobic

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62
Q

leucine functional group

A

aliphatic

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63
Q

isoleucine side chain properties

A

nonpolar/hydrophobic

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64
Q

isoleucine functional group

A

aliphatic

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65
Q

histidine side chain properties

A
  • positive/hydrophilic
  • can be positive or neutral at physiological pH
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66
Q

histidine functional group

A

imidazole ring

67
Q

cysteine side chain properties

A
  • polar
  • terminal sulfur + able to form disulfide bridges with other cysteines
68
Q

cysteine functional group

A

sulfhydryl

69
Q

proline side chain properties

A
  • nonpolar/hydrophobic
  • capable of self-bonding (bond forms between side chain and amino group)
70
Q

proline functional group

A

weird aliphatic (self-bonding creates a ring)

71
Q

methionine side chain properties

A

nonpolar/hydrophobic

72
Q

methionine functional group

A

aliphatic

73
Q

first amino acid in all polypeptides

A

methionine

74
Q

glutamate side chain properties

A

negative

75
Q

glutamate functional group

A

carboxylic acid

76
Q

aspartate side chain properties

A

negative

77
Q

aspartate functional group

A

carboxylic acid

78
Q

glutamine side chain properties

A

polar

79
Q

glutamine functional group

A

carboxyamide

80
Q

asparagine side chain properties

A

polar

81
Q

asparagine functional group

A

carboxyamide

82
Q

valine side chain properties

A

nonpolar/hydrophobic

83
Q

valine functional group

A

aliphatic

84
Q

tryptophan side chain properties

A

nonpolar/hydrophobic

85
Q

tryptophan functional group

A

aromatic

86
Q

serine side chain properties

A

polar

87
Q

serine functional group

A

hydroxyl

88
Q

threonine side chain properties

A

polar

89
Q

threonine functional group

A

hydroxyl

90
Q

tyrosine side chain properties

A

polar

91
Q

tyrosine functional group

A

hydroxyl

92
Q

lysine side chain properties

A

positive/hydrophilic

93
Q

lysine functional group

A

amino

94
Q

arginine side chain properties

A

positive/hydrophilic

95
Q

arginine functional group

A

guanidinium

96
Q

bonds in a polypeptide around which rotation can occur

A

phi & psi bonds

97
Q

bond in a polypeptide around which rotation cannot occur

A

peptide bond

98
Q

primary structure

A

a protein’s amino acid sequence

99
Q

secondary structure

A

alpha helices & beta pleated sheets

100
Q

pattern of hydrogen bonding in alpha helices

A

hydrogen bond occurs between carbonyl of amino acid i and i+4

101
Q

pattern of hydrogen bonding in beta pleated sheets

A
  • sheets stabilized by hydrogen bonding between 2-antiparallel beta strands
  • each amino acid forms 2 hydrogen bonds
102
Q

tertiary structure

A
  • protein folding into 3D conformation
  • driver by weak interactions
103
Q

quaternary structure

A

interactions between multiple polypeptides to form complex proteins

104
Q

orientation of bonds in parallel beta sheets

A
  • amino acid 1 bonds 2x to 2 other amino acids
  • forms 2x hydrogen bonds (one each)
105
Q

orientation of bonds in anti-parallel beta sheets

A
  • amino acid 1 bonds 2x to 1 other amino acid
  • it’s the like more even one but it’s antiparallel
106
Q

tertiary structure of myoglobins

A
  • myoglobins primarily in aqueous environment
  • hydrophobic amino acids oriented towards interior; hydrophilic on outside
107
Q

tertiary structure of porins

A
  • 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
Q

hemoglobin quaternary structure

A
  • 2 alpha globins + 2 beta globins = 4 linked polypeptides
  • heterotetramer (four non-identical amino acids)
109
Q

3 major differences between DNA & RNA

A
  • DNA = double helix; RNA = single-stranded
  • DNA ribose = no hydroxyl on 2’ carbon; RNA = additional hydroxyl group
  • DNA = thymine; RNA = uracil
110
Q

nucleoside

A
  • 5 carbon sugar + nitrogenous base
  • nucleotide without phosphate group(s)
111
Q

location of phosphodiester bond in nucleotides

A

5’C

112
Q

location of betaglycosidic linkage in nucleotides

A

1’C

113
Q

locations of bonds joining chains of nucleotides

A

3’OH - oxygen - phosphate - oxygen - 5’C

114
Q

chemical basis for stem-loop structures in RNA

A

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
Q

in DNA, antiparallel conformation facilitates _____

A

hydrogen bonding

116
Q

A-T base pairs form ___ hydrogen bonds

A

2

117
Q

C-G base pairs form ___ hydrogen bonds

A

3

118
Q

two types of chemical interactions which strengthen DNA molecules

A
  • hydrogen bonding (between base pairs)
  • van der Waal’s interactions (between “stacked” pairs)
119
Q

“lock and key” model of enzyme-substrate interaction

A

theory that enzymes naturally fit into active sites & enzyme conformation does not change

120
Q

induced-fit model of enzyme-substrate interaction

A

theory that bond with enzyme induces conformational change in enzyme which facilitates substrate binding

121
Q

4 types of interactions that can be occur between an enzyme & substrate in enzyme active site

A
  • hydrogen bonding
  • van der Waal’s
  • ionic interactions
  • hydrophobic interactions
122
Q

competitive inhibition ____ Vmax

A

does not affect

123
Q

competitive inhibition ____ Km

A

increases

124
Q

uncompetitive inhibition ____ Vmax

A

decreases

125
Q

uncompetitive inhibition ____ Km

A

decreases

126
Q

noncompetitive inhibition ____ Vmax

A

decreases

127
Q

noncompetitive inhibition ____ Km

A

does not affect

128
Q

3 fractions produced in cell fractionation by differential centrifugation

A
  • nuclear
  • mitochondrial
  • microsomal
129
Q

gel filtration chromatography

A

separates proteins according to size

130
Q

ion-exchange chromatography

A

separates proteins according to ionic charge

131
Q

affinity chromatography

A

isolates proteins via binding of a protein to a ligand capable of specific binding

132
Q

immunoprecipitation

A

used to isolate proteins

133
Q

co-immunoprecipitation

A

used to identify molecules which interact with protein of interest in the cell

134
Q

monoclonal antibody

A
  • identical copies of antibody
  • can bind antigen on one epitope (one antibody per antigen)
135
Q

polyclonal antibodies

A
  • antibodies capable of binding same antigen on different epitopes
  • can bind multiple antibodies per antigen
136
Q

sucrose bonds via a _____ glycosidic linkage

A

1,2

137
Q

lactose bonds via a _____ glycosidic linkage

A

1,4

138
Q

maltose bonds via a _____ glycosidic linkage

A

1,4

139
Q

bonds in cellulose indigestible by humans

A

beta-1,4

140
Q

____ is the major phospholipid from which most membrane phospholipids are derived

A

phosphatidate

141
Q

pepsin inactive form

A

pepsinogen

142
Q

pepsinogen activated by ____

A
  • HCl (partially activated)
  • pepsinogen
  • pepsin
143
Q

cholecystokinin (CCK)

A
  • digestive hormone
  • signals pancreas to release digestive enzymes
  • signals gallbladder to release bile salts
144
Q

secretin

A
  • digestive hormone
  • induces pancreas to release sodium bicarbonate
145
Q

trypsin zymogen

A

trypsinogen

146
Q

trypsin activated by ____

A
  • trypsin
  • enteropeptidase
147
Q

chymotrypsin zymogen

A

chymotrypsinogen

148
Q

chymotrypsin activated by ____

A

trypsin

149
Q

carboxypeptidase zymogen

A

procarboxypeptidase

150
Q

carboxypeptidase activated by ____

A

trypsin

151
Q

lipase zymogen

A

prolipase

152
Q

lipase activated by

A

trypsin

153
Q

alpha-amylase cleaves

A

alpha-1,4 bonds

154
Q

alpha-glucosidase cleaves

A

alpha-1,4 bonds

155
Q

maltase cleaves

A

alpha-1,4 bonds

156
Q

dextrinase cleaves

A

alpha-1,6 bonds

157
Q

maltase cleaves ____ to _____

A
  • maltose
  • 2 molecules glucose
158
Q

sucrase cleaves ____ to _____

A
  • sucrose
  • glucose + fructose
159
Q

lactase cleaves ____ to _____

A
  • lactose
  • glucose and galactose
160
Q

glucose and galactose are taken up into intestinal cells via _____, a form of active transport

A

the SGLT - sodium-linked glucose transporter

161
Q

fructose is taken up into intestinal cells via the ____

A

GLUT5 transporter

162
Q

glucose, fructose, and galactose are transported out of the cell via the ____

A

GLUT2 transporter

163
Q

CCK behavioral effects

A
  • increased satiety
  • decreased food intake
  • decreased body weight
164
Q

NAD+ is _____; NADH is _____

A

oxidized; reduced

BIOL 100 (3 decks)

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