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AH Biology > Unit 1 Key Area 2 > Flashcards

Unit 1 Key Area 2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the proteome

A

The entire set of genes expressed by the genome

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2
Q

Why is the proteome larger than the genes

A

Because more than one protein can be produced from one single gene as a result of the alternative rna splicing

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3
Q

What are genes called that do not code for proteins

A

Non coding RNA genes

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4
Q

What do non coding rna genes include

A

Those that are transcribed to produce tRNA, rRNA & RNA molecules that control the expression of other genes

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5
Q

The set of proteins can vary over time and under different conditions. What are these conditions

A

Metabolic activity of the cell
Diseased vs healthy cells
Cellular stress
The response to signalling molecules

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6
Q

What in eukaryotic cells increases the total area of membrane

A

System of internal membrane

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7
Q

do eukaryotes have a small or large SA:Volume ratio

A

RELATIVELY SMALL

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8
Q

What is a con of having a small plasma membrane

A

it hs too small for carrying out vital functions carried out by membranes

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9
Q

What is the endoplasmic recticulum

A

a network of membrane tubules continuous with the nuclear membrane

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10
Q

what is the golgi apparatus

A

a series of flattened membrane discs

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11
Q

what is a lysosome

A

membrane bound organelles cintaining a variety of hydrolases

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12
Q

what do hydrolases digest

A

Lipids, nucleic acids and carbs

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13
Q

what is a vesicle

A

it transports materials between membrane compartments

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14
Q

where are lipids and proteins synthesised

A

the endoplasmic reticulum

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15
Q

what is the Rough Endoplasmic reticulum

A

has ribosomes on its cytosolic face while smooth er lacks ribosomes

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16
Q

what happens with the lipids in the SER

A

inserted into its membrane

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17
Q

where does the synthesis of all proteins begin

A

the cytosolic ribosomes

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18
Q

where is the synthesis of proteins completed

A

the cytosolic ribosomes

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19
Q

where do the proteins remain after completion of synthesis

A

in the cytosol

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20
Q

what do transmembrane proteins carry

A

a signal sequence

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21
Q

what does a signal sequence do

A

halts translation and directs the ribosome synthesising the protein to dock with the ER

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22
Q

what does the docking of ribsomes form

A

the rer

23
Q

what is a signal sequence

A

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

24
Q

when does translation occur

A

continues after docking and the protein is inserted into the membrane of the ER

25
Q

What happens when the proteins are in the ER

A

they are transported by vesicles that bud off from the ER and fuse the golgi apparatus

26
Q

what happens in the golgi apparatus

A

the proteins move through the GA and they undergo Post translational modification

27
Q

what is the process for going through the golgi apparatus

A

molecules move through the golgi disc in vesicles that bud off from one disc and fuse to the next one in the stack.

28
Q

what do enzymes do in the golgi

A

catalyse the addition of various sugars in multiple steps to form the carbohydrates

29
Q

what is a MAJOR modification

A

the addition of carbohydrate groups

30
Q

what happens after the post translational modifications

A

the vesicles leave the golgi apparatus and take proteins to the plasma membrane and lysosomes

31
Q

where do vesicles also move to

A

move along microtubules to other membranes and fuse with them within the cell

32
Q

What is are examples of secreted proteins

A

peptide hormones and digestive enzymes

33
Q

where do secreted proteins begin translation

A

in ribosomes on the rer by entering its lumen

34
Q

what is the process of the secratory pathway

A

enter the rer lumen then move through the golgi apparatus (the normal protein synthesis occurs) the PTM occurs they are then packaged into secretory vesicles and the vesicles move to and fuse with the plasma membrane releasing the proteins out of the cell or move along microtubules

35
Q

what are many secreted proteins synthesised as?

A

inactive presursors

36
Q

what do inactive precursors require

A

proteolytic cleavage to produce active proteins

37
Q

what is proteolytic cleavage

A

another type of PTM

38
Q

why are digestive enzymes secreted proteins

A

if they were active within the cell it would be lethal for the cell and they require proteolytic cleavage to become active and carry out its function

39
Q

What do amino acids differ in

A

the R group present

40
Q

What do R groups vary in

A

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

41
Q

what are the r group classified as?

A

basic (+) acidic (-) polar and hydrophobic

42
Q

what does a diversity allow proteins to do

A

carry out a range of functionsw

43
Q

what is the primary function

A

the sequence in which the amino acids are synthesised into the polypeptide

44
Q

WHat does the secondary structure involve

A

hydrogen bonding along the backbone allowing the alpha helices, parallel or anti- parallell beta pleated sheets or turns to form

45
Q

what does folding of the polypeptide form

A

the tertiary structure

46
Q

how is the tertiary strucure stablised

A

with interactions between the r groups

47
Q

what is the quaternary structure

A

exists in proteins with twoor more connected polypeptide subunits

47
Q

what does the QS describe

A

the spatial arrangement of subunits

47
Q

what are disulfide bridges

A

covalent bonds between r groups containing sulfur

47
Q

ilhhd

what are examples of the interactions between the r groups

A

Ionic bonds
London Dispersion forces
Hydrogen bonds
hydrophobic interactions
Disulfide bridges

47
Q

what does a decrease in pH or increase in temperature do to the affinity of haemoglobin to oxygen

A

decrease affinity of haemoglobin for oxygen ∴ a reduced binding and this then causes the promotion of increases oxygen delivery to tissue

47
Q

what is a prosthetic group

A

a non-protein unit tightly bound to a protein essential for its function

48
Q

what is the ability of haemoglobin binding to O2 dependent on

A

the non-protein haem group

AH Biology (3 decks)

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