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1.2 : the proteome Flashcards

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1
Q

golgi apparatus

A

a series of flattened membrane discs that are connected to allow molecules to move

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2
Q

lysosomes

A

organelle which contain hydrolases to digest protiens, lipids and nucleic acids

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3
Q

vesicles

A

transport material between membranes along microtubules

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4
Q

what is the proteome

A

the entire set of proteins expressed by the genome.

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5
Q

endoplasmic reticulum

A

network of membrane tubules

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6
Q

rough endoplasmic reticulum

A

ER with ribosomes of ins cytosolic face.

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7
Q

smooth endoplasmic reticulum

A

lack ribosomes

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8
Q

what does a eukaryotes small size affect

A

will have a smaller surface area to volume ratio meaning the plasma membrane is too small to carry out its function so they must have a system of internal membranes which increases area

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9
Q

why is the proteome larger

A

more than one protien can be expresses due to alternate RNA splicing and post translational modification

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10
Q

factors affecting protein expression

A

metabolic rate, cellular stress, disease, response to signalling molecules

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11
Q

cytosolic protiens

A

synthesis begins in the cytosolic ribosomes and the synthesis is then also completed there and the proteins will remain in the cytosol

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12
Q

what are phospholipids and how are they synthesized

A

they are a lipid that forms the main component of cell membrane and they are synthesized in the SER and inserted into membrane

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13
Q

joining amino acids

A

through a condensation reaction, and a water molecule is made by taking OH from COOH of 1 amino acid and then the H from NH2 to form a peptide bond

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14
Q

classes of amino acids

A

acidic (- charge) = R group with COOH
basic (+ charge) = R group with NH2
polar (slight charge, hydrophilic) = with OH group
hydrophobic (no charge) = with hydrocarbon

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15
Q

why does R group detrmine amino acid strcuture

A

in an aqueous solution, NH2 will gain a hydrogen whereas COOH will loose a hydrogen meaning because of this neutral charge it is up to R group to determine structure and function

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16
Q

what do R groups vary by

A

size, shape, charge, hydrogen bonding capacity, chemical reactivity

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17
Q

what are the 4 groups bonded in amino acids

A

amine = NH2
acid = COOH
hydrogen atom
variable R group

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18
Q

polypeptide structure

A

a polymer of amino acids

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19
Q

why are R groups important

A

they determine protein structure and allows ligan to bind which determines location within the cell

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20
Q

primary structure

A

a poly peptide, the sequence in which amino acids are synthesized , this determines proteins functions

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21
Q

secondary structure

A

when polypeptide is folded into alpha helix, beta pleated sheet or a turn.
hydrogen bonds hold these structures together

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22
Q

what are the interactions for a tertiary structure

A

hydrophobic, ionic bonds, LDFs, hydrogen bonds, disulphide bridges

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23
Q

what is a disulphide bridge

A

covalent bonds between R groups containing sulfur

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24
Q

quaternary structure

A

exist in proteins with 2 or more subunits e.g collagen, hemoglobin

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25
Q

what is a prosthetic group

A

a non protein unit that is tightly bound to a protein and is necessary for its function

26
Q

what is proteolytic cleavage

A

this is a type of post translational modification that allows proteins to become active forms which will break the peptide bonds.

27
Q

what is a signal sequence

A

this is a short stretch of amino acids at one end of a polypeptide that determines the eventual location of the protein

28
Q

how are transmembrane protiens made

A

the synthesis begins in the cytosolic ribosomes, the transmembrane protiens made carry a signal that halts translation which directs the ribosomes synthesizing the protien to dock with the ER. translation continues after docking and protien is insterted into the membrane

29
Q

how does the movement of protiens occur

A

translation continues and the protien is inserted into the ER membrane it is then transported by vesicles which bud off from ER and fuse with Golgi apparatus and undergo PTM

30
Q

post translational modification process

A

this occurs when moving through the Golgi apparatus, enzymes will catalase the addition of carbohydrates to form glycoproteins which is the main modification, those vesicles which then leave the Golgi apparatus take the transmembrane protiens to plasma membrane and lysosomes and fuse them within the cell

31
Q

the secretory pathway

A

the protiens for secretion are then translated in ribosomes on the RER then enter its lumen, the protiens then move through the Golgi apparatus and are packaged into secretory vesicles they then move and fuse with plasma membrane and are released out of the cell many as inactive precursors

32
Q

what can influence R group interactions

A

tempreture and pH

33
Q

what does increasing tempreture do to R group interactions

A

raising the tempreture disrupts the interactions that hold the protiens shape which ultimately causes the protiens to denature

34
Q

how does pH affect R group interactions

A

pH only affects R groups that are acidic and basic, the normal ionic interactions become disrupted and charges are lost which gradually changes conformation and eventually denatures the enzyme

35
Q

what is haemoglobin

A

iron containing oxygen transporting protien present in red blood cells

36
Q

how to vesicles move

A

vesicles move along microtubules to other membranes

37
Q

what are inactive precursors

A

inactive precursors are inactive versions of protiens that require protealytic cleavage to become active

38
Q

tertiary structure

A

usually the final form, the poly peptide fold into a 3D shape and has conformation stabilised by R groups

39
Q

what is a ligand

A

a substance that can bind to a protien R group that is not involved with protien folding

40
Q

what does ligand binding change

A

ligand binding to a protein changes it conformation, this change in conformation changes the proteins function

41
Q

what is allosteric

A

interactions which occur in spatially distinct sites

42
Q

what does the binding of a substrate to an allosteric enzymes do

A

increases the affinity for all other active sites

43
Q

why do allosteric enzymes increase biological importance

A

because of the increase in affinity, this means that the activity of allosteric enzymes can change greatly with a small change

44
Q

what do allosteric protiens with many subunits show

A

cooperativity

45
Q

what is cooperativity

A

the binding at one subunit alters the affinity of the remaining subunits

46
Q

the second site in allosteris enzymes is

A

allosteric site

47
Q

what is the allosteric site

A

a separate site where modulators bind to regulate the enzyme activity

48
Q

what does the binding of a modulator do

A

changes the conformation and alters the affinity of the active site for the substrate

49
Q

positive modulators

A

increase affinity (activation)

50
Q

negative modulators

A

decrease affinity (inhibition)

51
Q

what is cooperativity

A

changes of binding at one subunit alter the affinity at others

52
Q

what shows cooperativity

A

oxygen and haemoglobin

53
Q

what is the binding of oxygen affected by

A

increase in tempreture and decrease in pH

54
Q

effect of pH on binding of oxygen

A

decrease in pH decreases the affinity for oxygen (moves to the right)
increase in pH increases affinity (moves to left )

55
Q

effect of temperature on binding of oxygen

A

decrease in temperature increases affinity for oxygen ( shifts to left )
increase in temperature decreases affinity ( shifts to right)

56
Q

addition or removal of a phosphate

A

a post translational method, the addition or removal of a phosphate causes conformational changes

57
Q

what are protien kinase

A

catalyses the transfer of phosphate group to other protiens. it is the terminal phosphate of ATP that is transferred to a specific R group

58
Q

protien phosphatase

A

catalyses the reverse reaction of phosphorylation

59
Q

what can phosporylation affect

A

brings about conformational change that effects protien activity, it regulates cellular protiens

60
Q

what does adding a phosphate do

A

adds a negative charge

61
Q

what happens to unphosphorylysed protiens

A

there ionic interactions can be disrupted and new can be created

advanced biology (6 decks)

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