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Cell Bio 360 > Nonono > Flashcards

Nonono Flashcards

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Biology 101 flashcards
1
Q

Binding pairs for COIP

A

GST: glutathione
Nickle: histidine
Streptavidin: biotin

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2
Q

Formula for max resolution

A

Lamda / 2

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3
Q

Forward genetics

A

Start with a desired phenotype and mutate a bunch of genes to see what happens

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4
Q

Reverse genetics

A

Mutate gene already chose to see the new phenotype and determine original phenotype

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5
Q

Cell fractionation via centrifuge.

A

Starts slowest: first pellet : whole cells, nuclei, cytoskeleton) medium ( mitochondria lysosomes and peroxosomes) fast ( microsomes and small vessicles / everything else small)

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6
Q

Velocity sedimentation

A

Uses sucrose base gradient which allows to further seperate after cell fractions

The fast sedement are more dense and go to the bottom first ie gel

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7
Q

What influences rigidity

A

Tail length, tail saturation, temperature.

Cholesterol helps mediate

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8
Q

Possible movement of phospholipids

A

Flexión: everyday movement constant
Lateral diffusion: changing spots with neighbors
Rotation: rotation in same spot
Flip flop: rare goes from one side to other side of membrane

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9
Q

What makes tail longer or shorter

A

Long tails (saturated)
Short tails ( unsaturated)

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10
Q

How to tell if transmembrane domain

A

20+ amino acid length (will be obvious)

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11
Q

How is protein mobility restricted

A

Scaffold proteins/ other cells
Fences
Seek to avoid or not leave lipid rafts

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12
Q

Transmembrane / peripheral proteins

A

Types of trans
Single pass (1 alpha helix) n terminus can be either side

Multiple pass ( more then one alpha)

Beta baroll ( hydrophobic beta sheet makes a channel through a membrane)

Peripheral
Anchored proteins ( via amphipathic alpha helix or post translation modified group added)

Auxiliaries don’t bind directly but bind to protiens bound to the membrane

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13
Q

Slowest step in actin poly

A

Nucleation waiting to form tetromer which is heavily regulated throughout the cell

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14
Q

Actin is a what ase

A

ATPase
As actin becomes old it moves down and taken off negative end and atp is changed to ADP

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15
Q

Cofilin

A

Causes breakage in actin and speeds up minus end disassembly
Lines sides

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16
Q

Tropomyosin

A

Stabilizes actin by lining sides of the filament

Inadvertently speeds up polymerazation

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17
Q

Formin

A

Mediates and promotes actin nucleation and elongation has arms to grab and put in place

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18
Q

Capz

A

Binds to plus end and prevents additions

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19
Q

Tropomodulin

A

Caps the - end prevents subtraction treadmill

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20
Q

Arp 2/3

A

Branching of actin filaments at 70

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21
Q

Thymosine

A

Binds to g actin and prevents it from getting added on

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22
Q

Profilin

A

Binds to g actin and makes it more likely to bind to plus end

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23
Q

Higher order actin structures

A

Bundle : multiple filaments stuck together

Cross linking ( intersections of actin not caused by 2/3)

Anchoring (bound to a surface and give strength)

Branching ( caused by 2/3)

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24
Q

Microtubule ase
And cytoskeleton structure

A

GTP
Beta over alpha
Spiral
13 circle

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25
Q

Microtubule proteins that assist in nucleation

A

Gama Tusc : makes 7 copy spiral that can be built off of

26
Q

Centrioles structure

A

Have a triplet 13 10 10
9 triplets around a sas 6 core

27
Q

Cilia flagella

A

Doublet microtubules
13 10 ring
9 doubles around two single 13 rings inside

28
Q

Centresomes mtoc

A

Two centrioles at 90 angle
Surrounded by pericentriolar material
Which is where gama tubulin rings like turc are which inciate nucleation

29
Q

MAPS

A

Stabilize microtubule by binding along sides helps prevent catastrophic

30
Q

Kinesin 13

A

Induces catastrophic and dissemble of micro tube plus side

31
Q

XMAP 215

A

Stabilizes plus end and accelerates assembly

32
Q

Y turc

A

Gamma tubulin ring nucleares assembly and remains on minus end

33
Q

Y tusc

A

Small complex form together rot make 13 slots to help nucleation to occur

34
Q

Can intermediate filaments form dimers

A

Yes yes they can

35
Q

What makes intermediate filiaments replaceable

A

Phosphorylation

36
Q

Protofilament

A

Monomer that come together to make diner protofibrals
Can be added on at both sides

37
Q

Keratins

A

Epithelium
IF
Give strength

38
Q

Neuro filaments

A

Help the axon grow
Streagth en crosssection

39
Q

Nestin

A

Also in neuron
Helps to maintain width
IF

40
Q

Lamins

A

Makes a mesh framework in nucleus
IF

41
Q

Vimentin

A

Involved in cell signals / tight junction
IF

42
Q

Dynein

A

Processive
Minus end
MT

43
Q

Kinesin

A

Processive
Plus end
MT

44
Q

Myosin 1

A

Non processive
Plus ended
(Vessicles transport)

45
Q

Myosin 2

A

(Non processive )
Plus end
Muscle contraction

46
Q

Myosin 5

A

Processive plus end motor
Involved in vessicles trans

47
Q

Myosin 6

A

Processive minus end
Vessicle trans

48
Q

Hemidesmosmes

A

Use integrins
Like intermediate filaments
Via integrin dimers and plectin adapters

Cell to matrix junction
Laminin and collagen

49
Q

Focal adhesión

A

Use integrins
Link integrin dimers to actin through talin and vinculin
Cell to matrix

50
Q

Desmosomes

A

Uses cadherins
Bound to Inter fill via plaques
Cell to cell jubction laminin and collagen

51
Q

Adherins junctions

A

Use cadherins bound to actin via alpha beta catenins
And vinculin (adapting protien)
Cell to cell jubction)

52
Q

How are integrins activated

A

RAP1 which is a GTPase
Binds RIAM and recruits adapter proteins

Active not holding hands
Inactive holding hands

53
Q

Cadherin activation

A

Adhering that bind in the presence of Ca
Most are homophonic

54
Q

Tight junctions

A

Made up of Claudins and occludins
Make a ring around the cell and make a tight seal

Don’t bind to cytoskeleton
And therefore can’t help tissue strength but instead fill gap

55
Q

Who do snoRNPs do

A

They methylate and pseudouridylation something

56
Q

Order of 45s maturation

A

Chemistry change by snoRna and then cleaved into 3 parts

28s 5.8s to 60s
18s to 40s
5 s goes to 60 but made elsewhere

57
Q

Space between 2 lipid layers of nucleus

A

Peri nuclear space
Lumen of ER

58
Q

The nucleolis location and structure

A

Mostly euchromatin with ribosome portiens and chaperone proteins

It is fused with nuclear membrane

59
Q

Linc complex

A

Outside Nesprin2: which interacts with cytoskeleton
Emerin sun : forms link From inside to outside and incudes nuclear lamina which binds transcription depressors
Enron and sun also bind BAF
BAF binds to chromatin

60
Q

How do lamins affect transcription what proteins are close by

A

They form chromosome scaffold to hold dna at specific places which impacts the amount of transcription that occurs in a certain region. Holds lamin A B1 B2 C and forms a network and is part of linc complex

Cell Bio 360 (2 decks)

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