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BSCI170 > Exam 2 > Flashcards

Exam 2 Flashcards

1
Q

exergonic

A

energy released ΔG<0

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2
Q

endergonic

A

energy added ΔG>0

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3
Q

Activation energy (Ea) with enzyme

A

lower than Ea without enzyme

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4
Q

activation energy (Ea) on a graph looks like

A

arrow from reactants to vertex

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5
Q

Free energy (ΔG) on a graph looks like

A

arrow from reactants to products

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6
Q

3 ways in which enzymes can lower activation energy

A
  1. physical strain
  2. orientation
  3. chemical change
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7
Q

catalyst

A

accelerate reactions without being consumed or permanently changed

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8
Q

saturation

A

rate of product formation is maximal.

carrier proteins can be this

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9
Q

3 ways to regulate chemical reactions

A
  1. operate enzymes under optimal conditions (temp, salt concentration, pH)
  2. inc. # of enzymes
  3. inhibitor molecules bind to enzyme - dec rate of product formation
  4. use regulatory molecules to stabilize the conformation and activity of the enzyme in 1 of 2 possible states
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10
Q

Irreversible inhibitors

A

Irreversible covalent attachment to enzyme usually at active site

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11
Q

Reversible competitive inhibitors

A

reversible noncovalent attachment to enzyme - active site binding

mimics shape of substrate, effects can be reduced by inc concentration of substrate

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12
Q

Reversible noncompetitive inhibitors

A

reversible noncovalent attachment to enzyme - non-active site binding

changes structure of enzyme; reduces normal function of enzyme

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13
Q

allosteric activator

A

stabilizes enzyme in active conformation

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14
Q

allosteric inhibitor

A

stabilizes enzyme in inactive conformation

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15
Q

covalent modification - phosphorylation

A

adds a phosphate group

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16
Q

feedback inhibition

A

metabolic pathway turned off by an enzyme at the front of pathway binding to end product when there is a lot of end product

stops cycle

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17
Q

mmol in a mol

A

1000 mmol = 1 mol

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18
Q

c in Π = cRT

A

osmolarity/concentration (mol/L)

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19
Q

T in Π = cRT

A

temperature (K)

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20
Q

R in Π = cRT

A

gas constant (.0821 L atm/Kmol)

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21
Q

Π in Π = cRT

A

osmotic pressure
atm

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22
Q

carbohydrates

A

attached to outer surface of proteins or lipids

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23
Q

integral membrane protein

A

span entire membrane or partially embedded

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24
Q

anchored protein

A

covalently bonded to lipids that are inserted into the membrane
no exposed hydrophobic regions

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25
Q

peripheral membrane protein

A

have polar or charged molecules that interact and noncovalently attached to either membrane surface

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26
Q

cholesterol

A

alters membrane fluidity, little yellow balls inside phospholipid bilayer

soluble in hydrophobic core
inc melting point - less fluid at high temp
interferes w phospholipid aggregation and stiffening - more fluid at low temp

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27
Q

outside of cell

A

carbohydrates stick out into it

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28
Q

inside of cell

A

anchored membrane proteins stick into it

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29
Q

diffusion

A

net movement of molecules from an area of higher to areas of lower concentration (randomness)

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30
Q

equilibrium

A

no net directionality to movement (still always movement)

concentration across membrane equal

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31
Q

osmosis

A

passive movement of water across a membrane to balance different solute concentrations

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32
Q

osmotic pressure

A

pressure that needs to be applied to a solution to prevent the flow of water across a membrane by osmosis

contributed to by presence of charged and large polar molecules

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33
Q

osmolarity

A

total # of solute particles per liter of water (concentration of solute particles)

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34
Q

faster diffusion

A

smaller molecules
hydrophobic, nonpolar molecules
higher temp
greater concentration gradient
larger surface area of membrane
shorter distance to traverse

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35
Q

O2

A

small nonpolar molecules
readily cross cell membrane

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36
Q

CO2

A

small nonpolar molecule
readily cross cell membranes

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37
Q

H2O, urea

A

small polar molecule
can cross cell membrane, permeability lower

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37
Q

ion

A

polar
cannot cross membrane, too hydrophilic

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38
Q

Isotonic solution

A

solution outside. cell has the same concentration as within cell
equilibrium

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39
Q

Hypertonic solution

A

solution outside cell has a higher solute concentration that within the cell

net movement of H2O is out of cell

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40
Q

Hypotonic solution

A

solution outside cell has lower solute concentration than within cell

net movement of H2O into cell

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41
Q

charge of magnesium ion (Mg)

A

+

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42
Q

charge of chloride ion (Cl)

A

-

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43
Q

electrons in carbon

A

6, 4 valence electrons

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44
Q

electrons in hydrogen

A

1

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45
Q

why is a bond nonpolar?

A

very small difference in the electronegativity of carbon and hydrogen

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46
Q

potassium (K) charge

A

+

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47
Q

Chlorine (Cl) charge

A

-

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48
Q

passive diffusion

A

for smaller hydrophobic molecules; simple diffusion

no energy or membrane protein required
CO2, urea

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49
Q

facilitated diffusion

A

membrane proteins (some integral membrane proteins) can aid in transport of polar or charged molecules

moves with concentration gradient
no energy required
specificity
various ions, flucose

50
Q

facilitated diffusion examples

A

carriers and channels

51
Q

active transport

A

energy added, against concentration gradient

allows cells to generate and maintain diff concentrations of substance across membrane
various ions

52
Q

cotransport

A

move more than one substance at a time

passive or active

53
Q

What type of transport is the Na+/K+ ATPase pump

A

primary active transport

54
Q

type of pores, specific or nonspecific bidning, what it transports

transport proteins - channels

A

hydrophilic pores; no specific binding
rapid movement of ions and water

55
Q

specific or nonspecific binding, speed (+ why), what it transports

transport proteins - carriers

A

specific binding of solute like an enzyme
requires a conformation change so its slower

glucose transport

56
Q

primary active transport

A

energy from ATP hydrolysis used to pump solute across a membrane to area of higher concentration

ADP + water –> ADP + phosphate ion

57
Q

primary active cotransport

A

ATP hydrolysis can provide the energy to actively move 2 solutes

58
Q

symport

A

cotransport where 2 substances moved to same side of membrane

59
Q

antiport

A

cotransport where 2 substances moved to different side of membrane

60
Q

uniport

A

1 substance transported; not cotransport

61
Q

& what type of protein does it use, what does it transport

secondary active cotransport

A

energy released from movement of one solute can assist in the movement of another solute again concentration gradient

cotransporter membrane protein

transports sugar and amino acid

62
Q

how is glucose transported against concentration gradient

A

secondary active transport - uses movement from Na+ in Na+-K+ pump

63
Q

exocytosis

A

secretion or release of material outside cell

64
Q

phagocytosis

A

cellular eating
cell extends cytoplasm to engulf material

65
Q

pinocytosis

A

cellular drinking
bringing fluid and dissolved substances into cell

66
Q

receptor-mediated endocytosis

A

brings specific molecules into cells
ligands bind to specific receptors

67
Q

clathrin

A

coating on the vesicle

68
Q

cyanobacteria

A

contains chlorophyll and therefore an autotroph

69
Q

archaea

A

lives in extreme conditions and is a seperate group because it resembles both bacteria eukaryotes

70
Q

where are membrane bound organelles found

A

only eukaryotes

71
Q

3 differences between plant and animal cells

A

plant cell has cell wall, large central vacuole, chloroplasts (autotrophs)

animals are heterotrophs with irregular shape, numerous small vacuoles, centrosomes, lysosomes

72
Q

what size of surface area-to-volume ratio is favored

A

larger

73
Q

what type of cells are favored

A

small cells

74
Q

what does surface area determine in cells

A

rate at which resources can enter and waste can leave

75
Q

what does volume determine in cells

A

amount of metabolic activity

76
Q

cytoplasm

A

everything within a cell membrane excluding nucleus; mostly water

77
Q

cytosol

A

gel like substance in cytoplasm

78
Q

organella

A

subcellular compartments in cytoplasm

79
Q

cytoplasmic inclusions

A

non-membrane bound substances

80
Q

nucleus

A

contains most of cell’s DNA

81
Q

what is the nucleus surrounded by

A

nuclear envelope

82
Q

what does the nuclear envelope have

A

nuclear pores

83
Q

nucleolus

A

region in nucleus where ribosomes are formed

84
Q

Endoplasmic Reticulum (ER)

A

network of interconnected membranes; high surface area

85
Q

lumen

A

interior compartment in ER

86
Q

Rough Endoplasmic Reticulums

A

outer membrane studded w ribosomes that synthesize proteins for secretion

once inside, proteins are chemically modified and transported to other locations

87
Q

smooth Endoplasmic Reticulum

A

connected to rough ER, lacks ribosomes

lipid synthesis, Ca2+ storage, detoxification of small molecules

88
Q

Golgi Apparatus

A

processes and packages material for secretion

protein and lipid secretion

89
Q

lysosomes

A

digestion autophagy (programmed destruction)

holds digestive enzyme and merges with food vacuole

90
Q

mitochondrion

A

oxidation of carbohydrates, lipids, proteins to produce ATP

91
Q

Chloroplasts

A

type of plastid
photosynthesis, food production
believed to have arisen from cyanobacteria

92
Q

peroxisomes

A

accumulate and break down toxic peroxide byproducts

93
Q

glyoxysomes

A

convert stored lipid to carbohydrates in plants

94
Q

vacuoles

A

largest plant organelles
store toxic and waste byproducts, contain pigments that attract pollinators, have catabolic enzymes (lysosomes)

95
Q

cytoskeleton

A

meshwork of protein polymers
maintains cell shape and position of internal constituents, interacts w extracellular structures to anchor cell in place

96
Q

microfilaments

A

actin protein, actin monomers can be added or removed

in cytoskeleton; maintain overall cell shape and cause localized changes in cell shape

cell movement; pseudopodia, muscle contractions, “pinching” contractions when animal cell divides

97
Q

intermediate filaments

A

anchor cell structures in place in cytoskeleton
keratin

monomers cannot be aded or removed

98
Q

what does it do, what’s it made of, can monomers be added/removed

mictrotubules

A

form rigid skeletons for some cells in cytoskeleton

can help move “cargo”

made up of tubulin (a and B) proteins

tubulin monomers can be added/removed

99
Q

cell junctions

A

cells joined through these

100
Q

tight junctions

A

prevent substances from moving through spaces btwn cells

epithelium of urinary bladder prevents urine from leaking into adjacent abdomen

101
Q

desmosomes

A

hold adjacent cells together w stable protein connections

permit some materials to move

mechanical stability for skin and other tissues under movement stress

102
Q

gap junctions

A

channels that run between membrane pores in adjacent cells

allows ions, small molecules, and electrical signals to pass between cells

heart muscles beat in unison

103
Q

juxtacrine

A

signaling between adjacent cells w physical contact

signals diffuse between cells through gap junctions and plasmodesmata or a membrane-bound signal binds to membrane receptor

104
Q

panacrine

A

btwn nearby cells

signals bind to receptors on nearby cell receptors

105
Q

autocrine signaling

A

signals bind to receptors on the same cell that secretes them

106
Q

Transmembrane protein receptors
(hydrophilic signals): Ligand-Gated Ion Channel

A

Cell membranes of many cells contain ligand-gated channels for ions like Na+, K+, Ca2+, Cl-.
* These protein channels/receptors
depend on ligand binding
* Ligands can be neurotransmitters (ACh, GABA, glutamate, epinephrine,
dopamine, serotonin, etc.)

107
Q

Transmembrane protein receptors
(hydrophilic signals): G-protein coupled receptor

A
  • Especially important in sensory systems
  • coupled with a G-protein
    that can bind GDP or GTP
  • seven hydrophobic
    membrane-spanning regions while G
    proteins have three subunits (α, β, γ)
108
Q

Transmembrane protein receptors
(hydrophilic signals): protein kinase receptor

A
  • Abundant and have enzymatic activity
  • Changes in receptor conformation on β subunits
    from α bonding to insulin (signal)

activates the cytosolic region of the
receptor, which has protein kinase
activity (adds phosphate groups here)

  • It adds phosphate group (obtained from ATP) to certain amino acids on proteins
109
Q

endocytosis

A

important role in feeding for unicellular eukaryotes

110
Q

do prokaryotes undertake endocytosis or exocyotisis

A

no, they release enzymes extracellularly to break down food

111
Q

endocrine signals

A

hormones

transported by circulatory system (w a vessel) and bind to receptors on distant cells

112
Q

Covalent Modification - dephosphorylation

A

removes a phosphate group

113
Q

covalent modification - proteolytic cleavage

A

amino acids removed (inactive enzyme becomes active)

114
Q

enzyme that adds a phosphate group from ATP to a protein

A

Protein Kinase

115
Q

What does addition and removal of phosphate groups signify?

A

addition - activates enzyme
removal - inactivation of enzyme

116
Q

name of enzyme involved in cAMP generation

A

Adenylyl Cyclase

117
Q

name of the enzyme that ceases the activity of cAMP

A

phosphodiesterase
(PDE)

118
Q

Intracellular Response

A

Receptors found in the
cytoplasm or nucleus
* Signal must be primarily
hydrophobic or very
small to diffuse through
the membrane.

119
Q

enzyme that removes a phosphate group from a protein

A

Protein Phosphatase

120
Q

Concentration of Na+ and K+ in outside in Na+/K+ ATPase pump

A

high Na+ concentration and low K+ concentration

121
Q

Concentration of Na+ and K+ in inside in Na+/K+ ATPase pump

A

low Na+ concentration and high Na+ concentration

122
Q

Steps of Na+/K+ ATPase pump

A
  1. 3 NA+ and 1 ATP bind to protein pump from inside of cell
  2. hydrolysis of ATP releases ADP and phosphorylates (amino acid) into pump of protein
  3. change in shape causes Na+ ions to be released outside cell and 2 K+ to enter + bind to pump
  4. 2 K+ binds to pump
  5. dephosphorylation of pump releases phosphorylates (pi) causing 2 K+ ions to be released into interior of cell
  6. returns pump to original form
  7. cycle repeated

BSCI170 (3 decks)

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