Cell Mechanics unit Flashcards

1
Q

What is cell fractionation (4 steps )

A

Method to take apart a cell to study function
1 homogenization
2 centrifuge
3 decant supernatant
4 repeat centrifuge increase speed, time

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2
Q

What are 2 main processes in cell franctionation

A

homogenization - disrupt cell membrane without damaging organelle
centrifuge - spin it to separate based on density

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3
Q

Main types of homogenization methods 4

A

use sound - high frequency
add detergent, good at pulling apart lipid
high pressure - force cells through small hole
shear - shear cells between rotating plunger and thick walls of vessel (like mortar and pestle)

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4
Q

Why is centrifugal step repeated what changes

A

repeated to separate each thing by density
what changes is the speed (increase) time, (increase`)

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5
Q

supernatant vs pellet

A

supernatant - lighter stuff, in liquid above pellet
Pellet - denser stuff on bottom
from centrifuge

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6
Q

Fluid mosaic model (meaning, devs)

A

dev by singer and nicholson (1972)
fluid -means movement in membrane
Mosaic - membrane is made from many diff molec

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7
Q

orientation phospholipids in cell membrane

A

polar head facing outside,
non polar hydrophobic end inside
makes bilayer with hydrophobic core
Each layer Is leaflet
because cell int and ext are both polar

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8
Q

polytopic vs monotobic

+ 2 subcatagories

A

Polytopic - faces both sides of membrane
Multipass - crosses membrane twice
Single pass - crosses membrane once
monotopic - does not span whole bilayer
for integral proteins

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9
Q

integral vs peripheral proteins

A

integral - can be poly/monotopic
if poly, can be multipass or single pass
Peripheral - noncovalently bound to one side of membrane , does not go in, can have same function as integral protein

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10
Q

Function of membrane protein (6)

A

signal receptor
enzymatic activity
recognition
attachment
transport
cell adhesion

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11
Q

What does receptor protein do

A

has binding site for ligand
once bonded to ligand
does conformational change
sends message to int of cell

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12
Q

What is ligand

A

thing that bonds to receptor protein

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13
Q

what does enzymatic activity membrane protein do

A

has binding site like enzyme
takes in substrate
changes substrate to new product

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14
Q

what does Recognition protein do

A

can be peripheral
recognizes glycoprotein of other cells

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15
Q

What is glycoprotein

A

carbohydrate group on surface, used to identify cell

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16
Q

Uses of carbs on surface of cell

A

Cell recognition and signalling
Glycoprotein - receptors for chem signaling
glycolipid- used in cell recognition

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17
Q

What do attachment proteins do
(2 types )

A

Extracellular (integral) - attached to ECM (Exterior extracellular matrix), does not move, for structural support, cell signaling, anchoring
Intercellular (inner peripheral or integral )- attached to cytoskeleton, anchored

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18
Q

What does exterior extracellular matrix do

A

cell structure
anchored to cell
used in cell signalling
has glycoproteins

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19
Q

what does intracellular cytoskeletal protein do

A

attachment protein
can be peripheral on interior
attached to cytoskeleton
anchored, immoble

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20
Q

3 main components of cytoskeleton, org by size

A

(microfilament) actin (smallest)
intermediate filament
(microtubules) - tubulin

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21
Q

Types of transport proteins and def

A

channel - passive, tunnel
- Gated
- ungated
Pump/carrier - like revolving door, conformational change

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22
Q

what are the 3 main forms of cell adhesion

A

channel forming junction
occluding(tight) junction
anchoring junction

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23
Q

Describe channel forming junctions, gap junction

+ example

A

makes channel between cells to pass small molecules
found in plants
makes keeps gap between cells

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24
Q

Describe occluding, tight junction

A

fuses membranes on adjacent cells
tight, no space between
makes impermeable barrier
found in digestive system
only O and CO2 passes
found by putting dye in and seeing where it cant penetrate

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25
Describe Desmosome, ANchoring proteins
bind to desmosomes in adjacent cell makes strong sheets attached to cytoskeleton to resist shear forces, mech strength bladder tissue
26
Functions of peripheral protein
Attachment recognition
27
What affect membrane fluidity
saturation of fatty acid hydrophobic restriction cholesterol, temp
28
Saturated vs unsaturated fatty acids for fluidity
unsaturated fatty acids keep the membrane more fluid makes it harder to compact the membrane,
29
Types of movement within mebrane (5)
Lateral - on same leaflet rotation - when molecs rotate around axis swing - tails swing from side to side flextion - contractile movement of tails Transverse diffusion - whole phospholipid switches side
30
WHat is transverse diffusion
related to hydrophobic restriction phospholipid moves from one leaflet to another with enzyme flippase rare because polar head must cross hyrophobic core
31
Why cholesterol helps fluidity
large, non polar effect depends on temp warm temp - makes less fluid by restricting movements of phospholipid cold temp - gets in the way of compacting the bilayer
32
what is the importance of cholesterol in cell
Structure regulates fluidity
33
WHen to use diff types of membrane transport
Passive - when goes with conct gradient Active- when goes against concentration gradient bulk membrane - for large moleculs
34
What is passive transport
No energy used go from high concentration to low concentration area
35
Simple diff vs facilitated diff
Simple - does not need protein, for O2 and CO2 - until equilibrium is achieved Facilitated diffusion - needs transport protein (carrier, channel)
36
Channel protein vs carrier protein
Channel - tunnel, some have swing gate - for ions (small charger molec) Carrier - revolving door, conformational change - can moves charged or uncharged (glucose)
37
What are the proteins needed for osmosis
Osmosis is passive transport needs aquaporins
38
Uniport, symport, antiport | definitions/example
Uniport - moves one thing at a time - channel prot Symport - moves 2 things at a time same direct - Na/glucose symporter Antiport - moves 2 things diff direct at time - Na/K pump
39
Describe water movement direction
goes from high concentration of water to low concentration moves in direction of dilute to solute moves in opposite direction of solut
40
Hypotonic meaning, effect on plant, animal, RBC
Outside env lower solute cont than inside solute moves out water moves in animal cell could burst (osmotic lysis) RBC - hemolysis Plant cell is good (turgid)
41
Hypertonic meaning, effect on plant, animal, RBC
More solute conct on outside than inside solute moves in water moves out animals cell shrivels RBC - crenation plant cytoplasm shrinks away from cell wall (plasmolysis)
42
Isotonic meaning, effect on plant, animal, RBC
Same concentration of solute in and out animal cell is good RBC is at equilibrium PLant - flaccid
43
WHy is osmosis important in CFTR (cystic fibrosis transmembrane conductance regulator )
Good CFTR takes chlorine out Bad CFTR builds up concentration of chlorine in cell draws in more water with osmosis less water on outside causes mucus to form
44
Active- vs passive transport
Passive - no eng needed - goes with cont gradient Active- - needs eng (ATP) - goes against cont gradient - needs pump (like carrier prot)
45
How is builk membrane transport diff from other types
Does not use transport protein for large molecules for large amts involces folding of membrane to make vesicle
46
Types of bulk memb transport
endocytosis - pinocytosis - phagocytosis - receptor mediated endocytosis exocytosis
47
What is phagocytosis | + examples in ppl and other
"eating" of cell ingest other cells or large particles uses vacuoles amoebas use to eat used to humans to defend body ex phagocyte (WBC)Ha
48
Mechanism of phagocytosis | 6 steps
1 cell engulfs molecs with **Pseudopodia** 2 encloses molecs in **Vacuole** called **phagosome** 3 Lysosome fuses with it to become **phagolysosome** 4 lysosome digests the stuff inside 5 leaves behind **residual body** 6 vacuole disposes of res body outside
49
What is pinocytosis
"drinking" of cell uses vesicles for dissolves materials(smaller stuff) anything can be ingested
50
Phagocytosis vs pinocytosis
Phago - for large molec, makes large vacuoles Pino - for small molec, makes vesicle
51
What are the steps in receptor mediated endocytosis
Ligand binds to receptor membrane becomes vesicle ligand detaches from receptor vesicle pinches into 2 parts - empty receptors - ligand Ligand part fuses with lysosome receptors return to cell surface
52
What is exocytosis
movement of materials from inside to outside of cell vesicles come from golgi body reverse of endocytosis
53
What are the 3 main functions of exocytosis
restoring cell membrane - keep up with endocytosis secreting - release waste and toxin from cell recycling of membrane proteins (receptors )
54
What are the types of enzymes | hint: cofactor or not
SImple - only has protein component COmplex - requires a cofactor in addition to protein body, Has 2 forms (apoenzyme, holoenzyme)
55
Apoenzyme vs holoenzymes meaning
States of complex enzymes apoenzyme is inactive state due to not having cofactore holoenzyme is active form of enzyme with cofactor
56
What are the types of cofactors (2 + 2)
Inorganic - metal ions (Zn, Cu, Fe) organic - vitamins in addition, they can be - prosthetic - permanently bonded to enzyme (Heme ) - coenzyme - reversible bonded to enzyme (NADH)
57
what is enzyme (def, component)
Usually made from protein Catalyst, speeds up reaction is reusable decreases activation energy ends in -ase (sucrase) can create or reverse productW has active site - substrate area enzyme only works on specific substrate
58
What is the induced fit model
As substrate binds the enzyme changes to tighter fit brings in chem groups to catalyze reaction binding induces favorable change in enzyme
59
What is free energy graph for (what does it display)
used for reactions that release energy shows how much energy is needed to start reaction energy given in heat eng amount it rises above beginning is Activation energy amount it goes below beginning energy is change in free energy ( Delta G)
60
What is Delta G in free energy graph
Difference in free energy between start and products Negative in exorgonic reactions new bonds release more energy than the initial investment to break bonds not changed by enzymes
61
What is Activation energy in free eng graph
The amount of eng needed to start the reaction enzyme lowers the act eng reactants absorb eng, becoming unstable until bond breaks
62
Mechns by which enzyme lower act eng (4)
1 proximity, orientation 2 bond strain - 3. microenvironment - R groups in enzyme make good env for reactants 4 covalent catalysis - bonds with reactants to help orient, change chem of active site
63
What limits enzyme and reaction rate
substrate concentration temp pH level availability of cofactors
64
What is an inhibitor
molecule that bonds to enzyme, stops it from doing job can be reversible depending on connection can be competitive or non competitive
65
Competitive vs non competitive inhibition
Comp - inhibitor binds to active site, directly blocks substrate non comp - inhibitor binds somewhere other than active site, changes the shape of enzyme to be ineffective
66
How does competitive inhibition affect saturation curv+ how to overcome
Makes curve less steep but reaches same height in the end add more substrate
67
How does non competitive inhibition affect saturation curv+ how to overcome
lowers plateau of curve add more enzymes
68
Why does inhibition exist naturally
used to regulate production of stuff, so as not to overdo product negative feedback
69
What is negative feedback
When the product is also the inhibitor of one of the enzymes in the chain that produces it cannot be inhibitor of last enzyme in chain
70
Characteristics of allosteric enzyme (4)
has second binding site, other than active site has 2 conformations (active, inactive) naturally oscillates between 2 conformations binding of effector can stabilize the shape
71
What is the allosteric site
Binding site other than active site can be found in between subunits (where they join)
72
What is an effector? (def, types)
Something that binds to allosteric enzyme binds weakly allosteric activator - stabilizes active form allosteric inhibitor - stabilizes inactive form (same as non competitive inhibition)
73
what is allosteric regulation
regulation enzyme activity with effector in allosteric site causes inhibition or Activation
74
What is cooperativity (conditions, )
when the binding of one effector in one subunit effects all other subunits only occurs in enzymes with multiple subunits can increase or decrease productivity
75
Negative vs positive cooperativity
pos - activator, in active site, allosteric (substrate binding, activator binding ) neg - inhibitor, only allosteric (some forms of noncomp inhibition)
76
does positive cooperativity need allosteric site
no one example of positive cooperativity is the substrate causes other subunits to become better for other substrates
77
allosteric inhibition vs negative cooperativity
allosteric inhibition can be negative cooperativity cooperativity must have many subunits AlloInhib does not both must have allosteric enzyme, involve allosteric site
78
What are the 6 classes of enzymes (order matters )
1. oxidoreductase 2. transferase 3. hydrolase 4. Lyase 5. isomerase 6. LIgase
79
What is Oxidoreductase (def, funct, react, ex)
First enzyme class F: shuffles electrons R: Redox reactiosn: electrons are moved around through transfer of H and O Dehydrogenase
80
What is transferase (def, funct, react, ex)
class 2 F : moves chem groups R : transfers phosphates and methyl to other substrate ex. polymerase
81
What is hydrolase (def, funct, react, ex)
class 3 F : breaks molecules with water R: hydrolysis reactions ex protease
82
What is lyase (def, funct, react, ex)
class 4 F : break molecules without water R: removal or addition of groups ex. decarboxylase
83
What is isomerase (def, funct, react, ex)
class 5 F: changing molec shape R: shuffling atoms around in molec Ex: mutase
84
What is LIgase (def, funct, react, ex)
class 6 F : forming bonds between molec R: Dehydration synthesis, joining 2 molecules Ex synthetase
85
Describe Na/K pump
Is active transport antiport has 2 conformational states 3 Na + go out ATP is used 2 K+ goes in
86