Ib bio > unit 9 > Flashcards

unit 9 Flashcards

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1
Q

water properties

A

-covalent bonds- unequal charge creates polarity
-high heat capacity-mainstains homeostasis and earth temperatures
-cohesion: sticks to itself- surface tension for habitat
-adhesion: sticks to other molecules- water sticking within body, movement up plant

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2
Q

covalent vs hydrogen bonds

A

covalent: within molecule
hydrogen: between molecules

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3
Q

why didnt water exist at start of earth according to hypothesis

A

the earth was too hot

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4
Q

where did water come from

A

asteroids that contained water and ice hit earth
the earth was cooled from the water’s high heat capacity

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5
Q

what does goldilocks zone mean

A

earth is the perfect distance from sun to keep water a liquid
-helps search for life on other planets by comparing sizes and distances

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6
Q

amino acid structure

A

Central carbon
carboxyl- cooh
hydrogen
r group
amine group- NH2

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7
Q

how are amino acids connected

A

by peptide bond between amine and carboxyl groups

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8
Q

what creates diversity of amino acids

A

20 different r groups

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9
Q

categories of r groups

A
  1. non polar: hydrophobic
    -middle of protein so less exposed to water
  2. polar: hydrophilic
    -outside of amino acids
  3. charged vs non charged
    -charged: negative=acidic, positive= basic
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10
Q

what does primary structure mean

A

sequence of amino acids decided during translation from codon reading mRNA

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11
Q

what does location of amino acid mean in tertiary structure

A

determines how r groups interacts and what r groups are attracted to substrate of enzyme

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12
Q

what is a polypeptide

A

chain of amino acids connected by peptide bonds-doesnt do anything yet

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13
Q

what is a proteome

A

all of our specific proteins
-helps see mutations

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14
Q

what is secondary structure

A

3D shape that shows up-nothing to do with r grouos
comes from interactions of carboxyls and amine

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15
Q

what are the 2 shapes of secondary structure

A
  1. alpha helix
  2. beta pleated sheet
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16
Q

what is the secondary structure held together by

A

hydrogen bonds

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17
Q

what is tertiary structure

A

unique shape of polypeptide because of unique r groups from primary structure

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18
Q

bonds in tertiary structure

A
  1. ionic: transfer of electrons between - and + charged r groups
    -affected by pH
  2. hydrogen: polar to polar
  3. disuflide: only between r groups with sulfure(cysteine)
  4. hydrophobic: non polar r groups
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19
Q

what proteins might need to be ampipathic

A

membrane proteins

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20
Q

what proteins must be polar

A

channel proteins

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21
Q

what is quarternary structure

A

multiple polypeptides connecting to make protein- most proteins
-many different bond(exponentially increases possibilities of proteins)

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22
Q

what is a conjugated protein

A

protein has extra molecule attached at all times
-ex: hemoglobin-has heme group(mainly made of iron, mainly where oxygen is transported)

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23
Q

non conjugated protein examples

A

insulin, collagen

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24
Q

what are fibrous proteins

A

they dont have tertiary structure, they are mostly just polypeptides. they do have quarternary structure because it raps around other chains

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25
example of fibrous protein
collage: gives strength and structure in skin -has amino acids that prevent interactions of others -3 long polypeptides
26
globular proteins
3D shape, complex, obvious secondary and tertiary structures. -enzymes and receptor proteins -insulin
27
enzyme overview
speeds reactions, make life possible, turn substrate into products, decrease activation energy, specific pH and temperatures, made in ribosomes
28
intracellular enzymes
in cell, made by free ribosomes ex: helicase, polymerase, cell respiration enzymes
29
extra cellular enzymes
between cells, usually for digestion made by pancreas- has lots of rough ER
30
why do products usually have less energy than substrates
enzyme is not 100% efficient and energy is lost from bond movement and released as heat
31
what animals have adapted to maintain body temperatures
birds and mamals
32
heat negative feedback from exercise
excercise creates more heat from enzymes working and releasing energy, body cools by sweating
33
what animals have cells that are simply for releasing heat instead of producing energy
polar bears, walruses
34
what is a metabolic pathway
a chain of reactions
35
what are intermediate changes
changes between beginning and end product of pathway -product of reactions becomes substrate for next reaction
36
advantage to metabolism being multi-stepped
allows flexibility in process based on what it needs-can adjust process step by step
37
what is non competitive inhibition
inhibitor binds somewhere other than active site on enzyme changes shape of active site
38
what is the allosteric site
place on enzyme where inhibitor binds
39
what is competitive inhibition
inhibitor binds to active site no shape change -can be outcompeted by substrate concentration
40
competitive inhibitor example
statins: in medicine for people with high cholesterol -compete for enzymes in liver which produces cholesterol
41
what is feedback inhibition
end product becomes inhibitor for begining of enzyme pathway to slow more being made -usually non competitor-guarantees slowed process -as product is used up->less inhibitors, -> more being made
42
threonine into isoleucine end product inhibition
threonine is made into isoleucine by enzyme pathway. isoleucine goes back and becomes non competitive inhibitor by binding to allosteric site of threonine. threonine-non essential isoleucine-essential
43
what is mechanism-based inhibition
it irreversibly binds to active site meaning it destroys enzymes -toxins poisons, chemical weapons(novichok)
44
penicillin as mechanism based inhibitor
penicillin kills transpeptidase which is the enzyme that bacteria uses for cell walls -transpeptidase gains resistance because of mutations in DNA which leads to different amino acids which changes active site so that penicillin can no longer bind. passed down by natural selection.
45
what is oxidation
loss of electrons leading to increase in charge
46
what is reduction
increase of electrons and decrease in charge -adding hydrogen,adding electron
47
what does electronegative mean
oxygen in chemosynthesis is used to pull electrons from hydrogen
48
what happens when phosphate is added to molecule
energy is added molecule is more unstable and activated(more likely to react with another)
49
cell respiration formula
O2+C6H12O6-> CO2+H2O
50
where does glycolysis happen
cytoplasm
51
glycolysis steps
1. glucose is phosphorylated from ATP and takes 2 phosphates, which makes glucose unstable and split into 2 triosphosphates 2. 2 free floating phosphates(inorganic phosphates) connect to each triosphosphate. 3. Triosphosphates give up hydrogen-oxidation- to NADs which become NADH-reduced. 4. triosphosphates become pyruvate and all phosphate is given to ADP to make 4 ATPs
52
final products of glycolysis
2 NADH, 2 pyruvates, 4 ATP
53
when/where/why does anaerobic respiration happen
when there's no oxygen-stays in cytoplasm -our cells cant use pyruvate and NADH so we make NAD and NADP to make glycolysis repeat(fermentation)
54
what does fermentation make
lactic acid in humans -buildup causes soreness CO2 and ethanol in yeast -bread rise and alcoholic beverages
55
what is the link reaction
if oxygen is present, everything enters mitochondria 1. pyruvate enters matrix 2. pyruvate is decarboxylated-makes CO2 3. leftover 2 carbon molecule is oxidized-hydrogen given to NAD to make NADH 4. molecule is activate by coenzyme A attaching to it 5. acetyl a: C2H2O4- molecule made from link reaction along with CO2 and NADH
56
steps of Krebs cycle
1. oxaloacetate(4 carbon molecule in body) bonds to acetyl A after acetyl is activated-coenzyme goes back to link reaction 2. Citrate, the 6 carbon molecule formed is deoxylated twice. Oxidation happens at same time and Hydrogen is released 4 times to make FADH and 3 NADH 3. ADP becomes ATP from energy released 4. ends up with 4 carbons-cycle restarts
57
what is the point of electron transport chain(ETC)
to make 30 ish ATP
58
steps of ETC
1. when energy carriers NADH and FADH are oxidized, they give up high energy electrons that move from protein to protein in inter membrane space 2. when they move, energy is used to pump hydrogen through membrane into inter membrane space which creates concentration gradient for hydrogen to flow in using ATP Synthase 3. ATP synthase captures energy to put in ADP to make it ATP using inorganic phosphate 4. Terminal oxygen acceptor gets positive charge from hydrogen, negative from electron to create water
59
what is ATP synthase
enzyme used to synthesize ATP that hydrogen flows through
60
what is chemiosmosis
means that chemicals are used to set up concentration gradient-movement of molecules captures energy
61
adaptations of mitochondria
1. cristae:folds of inner membrane -increases surface area for room for ETC and ATP being made 2. intermembrane space -small-makes concentration of hydrogen very high to create gradient 3. matrix -big space to decrease concentration of hydrogen -more room for Krebs cycle and link reaction 4. outer membrane -controls what goes in and out(selective permeability -keeps mitochondria from being affected by heat
62
final products of glycolysis, link reaction, and Krebs cycle
6 CO2, 4ATP, 10NADH, 2 FADH
63
carbohydrates as energy sources
-produce pyruvate when broken down -soluble -can carry out anaerobic respiration -have more CO2 which causes more energy lost due to oxygen atoms -atp easier broken down
64
lipids as energy sources
-become fatty acids and acetyl groups when broken down -non soluble -can carry out aerobic respiration after-not anaerobic -mainly carbon and hydrogen- less CO2-less energy lost -More ATP that's harder to break down
65
what is a pigment
any molecule that abors some types of light and reflects others
66
what is chlorophyll
a pigment and protein -many different kinds even within 1 plant -arranged in circles-called array -located in thylakoids in chloroplasts
67
thylakoid membrane structure
folded to increase surface area
68
what is a granum
a stack of thylakoids
69
where are photosystems located
thylakoid membranes
70
what happens in the light dependent reaction in photosystem II
chlorophyll absorbs light. light molecules filter toward center of pigments called the reaction center where the electrons are energized. excited electrons ejected to be passed protein to protein until electrons get to next photosystem. electrons lost are replaced with electrons from water-splits water(photolysis) oxygen released into atmosphere. energy is used and hydrogen is pumped from stroma inside thylakoid to create concentration gradient. hydrogen flows out ATP synthase to make energy to be stored in glucose
71
light dependent reaction in Photosystem I
electron is reenergized by photosystem I. electron travels down short ETC to make NADP become NADPH
72
where does light independent reaction occur
in stroma
73
what happens in light independent reaction
Ribulose BisPhosphate(RuBP) is reacts with CO2 using RuBisCo-carbon fixation -RuBp splits into 2 G3P molecules -G3Ps get phosphate from ATP made in light dependent reaction -G3Ps reduced at same time by NADPH made in light dependent reaction - become triosphosphates -1/6 triosphosphates made go to make glucose or other carb -other 5 stay to do it again to regenerate 3 5-carbon molecules(RuBP)-uses more ATP
74
how many turns of calvin cycle make glucose
2
75
adaptations of the chloroplast
chloroplast enevelope(double membrane): -selective permeability: CO2 in, water in, light in(transparent), glucose and CO2 outt thylakoids: more surface area for light dependent reactions -cristae:increase SA even more small space inside thylakoids: increase concentration large stroma: large space for Calvin cycle starch droplets: made of glucose, how plant stores energy 70s ribosomes for DNA and proteins
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