Week 4 Flashcards

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1
Q

modifications to amino acids

A

phosphate, acetyl, sumo, ubiquitin, methyl

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2
Q

proteins are NOT

A

long linear molecules of amino acids

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3
Q

primary structure of protein
secondary
tertiary
quaternary

A
  • amino acid sequence. linked by peptide bonds.
  • stretches of polypeptide chain. alpha helix, b sheet. backbone hydrogen bonding
  • polypeptide chain. interactions of R groups
  • more than one polypeptide chain. noncovalent bonds of different chains
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4
Q

C reactive protein

A

binds to C polysaccharide. Donut as protein, made up of five individual amino acid chains. but you need 5 to have a functional C reactive protein.

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5
Q

every protein wants to be at its

A

lowest energy state.

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6
Q

A (unit)

A

angstrom. length.

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7
Q

beta sheet (strands)

A

parallel or antiparallel, form H bonds bw side chains

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8
Q

proteins share similar structures

A

domains = sequence of amino acids w diff structure/function.

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9
Q

some proteins may add

A

domains over the course of time (duplications). may have multiple domains

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10
Q

SH3

A

binds polyproline regions

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11
Q

SH2

A

binds phosphorylated tyrosine residues (Y^P)

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12
Q

kinase domain

A

phosphorylates (adds) proteins (can be tyrosine kinase or ser/thr kinase{bc of hydroxyl groups}) or lipids. has catalytic activity.

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13
Q

when the protein is in tertiary structure

A

it is at its lowest energy state.

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14
Q

protein structure functions

A
  • regulates activity-temporal and spatial activation (when and where to act) depending on structure
  • specificity of activity- act on “correct” substrates based on structure
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15
Q

intracellular trafficking/vesicular trafficking

A

vesicles move cargo from one place to another

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16
Q

endocytic pathway

A

-Normal pathway - early endosome to late endosome to lysosome
– Decreasing pH is imp for protein-protein interactions

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17
Q

what do lysosomes do in cell?

A

break down molecules that are brought to site so it can be used for amino acids, carbohydrates (food sources).
-acid hydrolases - proteins that cut

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18
Q

exocytic pathway

A
  • Transport of molecules from inside cell to the plasma membrane or elsewhere
  • ER to ergic to golgi to EE - LE -LYS (PM)
  • known as secretory or biosynthetic pathway
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19
Q

vesicular transport
3 steps
vesicular ____ ?

A
  • vesicle budding - coat proteins
  • vesicle transport - rabs, tethers
  • vesicle fusion - SNARES
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20
Q

3 main COAT proteins

functions?

A

-clathrin (in PM and some in GOLGI (away from trans golgi)
-COPI coat- ERGIC and GOLGI
-COPII coat- ER to ERGIC
Functions
-formation of vesicle, causes curvature
-concentration cargo

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21
Q

what needs to be curved?

A

membrane needs to curve around cargo

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22
Q

Clathrin made up of what?

A
  • 3 large polypeptides and 3 small polypeptides chains

- Triskelion

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23
Q

underside of plasma membrane

A
  • Forms into basketlike structure called a coated pit

- Causes curvature and concentrates cargo

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24
Q

Clathrin doesnt act alone

A
  • adaptin binds to clathrin, membrane, and transmembrane proteins-to help get them into coated pits (Concentrates cargo)
  • Different adaptins used (AP1, AP2 and AP3)
25
Q

why do we need 3 diff adaptin proteins?

A

all about specificity.

26
Q

ligand

A

protein that binds to another protein. changes its shape and function.

27
Q

protein that pinches off

A

clathrin and adaptin and dynamin

28
Q

dynamin

A

wrapped around membrane, known as GTPase.

29
Q

hydrolysis

A

cleave a phosphoanhydride bond

30
Q

adaptin has a lot of

A

polypeptides. whole thing is macromolecular assembly.

31
Q

GTPase

A
  • Class of proteins
  • Utilize binding of GTP/GDP-changes in conformation
  • Binding to GTP turns “on”
  • Hydrolysis of GTP to GDP turns “off”
32
Q

backwards-

forwards-

A
  • retrograde

- anterograde

33
Q

ergic can also be called

A

VTC-vesicular tubular cluster. From ERGIC,

vesicles bud and go to cisGOLGI

34
Q

Sar1

A

is GTPase. binds to gtp and hydrolyzes gtp to gdp

35
Q

ERGIC stands for

A

ER golgi intermediate compartment

36
Q

what sec proteins make up COPII?

A

sec 13/31, sec 23/24

37
Q

COPI

A
  • Retrograde transport from ERGIC to cis GOLGI
  • Retrograde transport from TGN back to CGN
  • CGN back to ERGIC and ER
38
Q

uncoating

A
  • happens quickly after budding
  • requires ATP
  • coats are removed
39
Q

when the clathrin and cargo buds off

A

it is called clathrin coated vesicle

40
Q

GTPase cycle

A

hydrolysis of water loses an inorganic phosphate. cleaves GTP and leaves it in GDP bound form, and GAP proteins help to speed up cleavage.

41
Q

GTPase cycle

how do you get it back to GTP?

A

enzyme that adds phosphate. GDP needs to come off so that GTP can bind. GEF bumps off GDP.

42
Q

without gap and gef

A

goes really slow

43
Q

GAP stands for

A

GTPase activating protein

44
Q

GEF stands for

A

guanine nucleotide exchange factor

45
Q

caax box

A

found at C terminus. (cystein, alanine, alanine,..). has to be there for lipid modification.
Ccxx - caax box has 2 sequences

46
Q

tethering molecules

A

loose interactions. low affinity.

47
Q

Snares stands for what

A

snap associated receptor

high affinity.

48
Q

rab proteins

A
  • C-terminal end
  • spatial specificity. helps vesicle move from one location to another through tether molecules.
  • GDP lipid tail tucked in
  • GTP lipid tail sticking out
49
Q

another name for late endosome

A

MVB. multi vesicular body

50
Q

of rabs in human genome

A

70

51
Q

snare proteins

A
  • Coiled-coil proteins
  • Bind in a 1:3 ratio of coils
  • v-SNARE and t-SNARE
  • R-SNARE (almost always v snares) and Q-SNARE (almost always t snares)
  • SNARE promiscuity - bind with many different SNARES in vitro
52
Q

in vitro

A

outside of its natural place.

53
Q

mechanism of SNARE fusion

A

Docking
Zippering
Membrane fusion
Cis-SNARE complex must be dissociated to regenerate trans-SNARE proteins

54
Q

rabs are in

A

endo and exocytic pathways

55
Q

delivery to lysosomes in 3 ways

A
  • phagocytosis-cells eat
  • autophagy- cells eat oneself
  • receptor mediated endocytosis
56
Q

lysosomes cut what?

A
  • protease-cuts proteins
  • lipases- lipids
  • glycosilase- glyocprotiens
  • nucleases - nucleic acids
57
Q

autophagy

A

removal of damaged organelles. membrane surrounds it, then delivered to lysosomes where it will be degraded

58
Q

protein get modified

A

addition of sugars or phosphate

59
Q

in the fusion step (SNARE), you need ____ to cleave off the cis snare complex so you can reuse it

A

NSF and ATP