Unit 1 Key Area 2 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

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
What happens when the proteins are in the ER
they are transported by vesicles that bud off from the ER and fuse the golgi apparatus
26
what happens in the golgi apparatus
the proteins move through the GA and they undergo Post translational modification
27
what is the process for going through the golgi apparatus
molecules move through the golgi disc in vesicles that bud off from one disc and fuse to the next one in the stack.
28
what do enzymes do in the golgi
catalyse the addition of various sugars in multiple steps to form the carbohydrates
29
what is a MAJOR modification
the addition of carbohydrate groups
30
what happens after the post translational modifications
the vesicles leave the golgi apparatus and take proteins to the plasma membrane and lysosomes
31
where do vesicles also move to
move along microtubules to other membranes and fuse with them within the cell
32
What is are examples of secreted proteins
peptide hormones and digestive enzymes
33
where do secreted proteins begin translation
in ribosomes on the rer by entering its lumen
34
what is the process of the secratory pathway
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
what are many secreted proteins synthesised as?
inactive presursors
36
what do inactive precursors require
proteolytic cleavage to produce active proteins
37
what is proteolytic cleavage
another type of PTM
38
why are digestive enzymes secreted proteins
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
What do amino acids differ in
the R group present
40
What do R groups vary in
size, shape, charge, hydrogen bonding capacity and chemical reactivity
41
what are the r group classified as?
basic (+) acidic (-) polar and hydrophobic
42
what does a diversity allow proteins to do
carry out a range of functionsw
43
what is the primary function
the sequence in which the amino acids are synthesised into the polypeptide
44
WHat does the secondary structure involve
hydrogen bonding along the backbone allowing the alpha helices, parallel or anti- parallell beta pleated sheets or turns to form
45
what does folding of the polypeptide form
the tertiary structure
46
how is the tertiary strucure stablised
with interactions between the r groups
47
what is the quaternary structure
exists in proteins with twoor more connected polypeptide subunits
47
what does the QS describe
the spatial arrangement of subunits
47
what are disulfide bridges
covalent bonds between r groups containing sulfur
47
# ilhhd what are examples of the interactions between the r groups
Ionic bonds London Dispersion forces Hydrogen bonds hydrophobic interactions Disulfide bridges
47
what does a decrease in pH or increase in temperature do to the affinity of haemoglobin to oxygen
decrease affinity of haemoglobin for oxygen ∴ a reduced binding and this then causes the promotion of increases oxygen delivery to tissue
47
what is a prosthetic group
a non-protein unit tightly bound to a protein essential for its function
48
what is the ability of haemoglobin binding to O2 dependent on
the non-protein haem group