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Unit 1: Cells and Proteins KA 1.2: Proteins Flashcards

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1
Q

describe how alternative RNA splicing allows for more than one protein to be produced from one gene

A

different combinations of coding regions called exons can be left in or removed during transcription to produce different mature RNA transcripts.

this allows different proteins with different structures and functions to be produced

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2
Q

the number and type of proteins produced by a cell can vary over time and are affected by various factors such as… (4)

A

-metabolic activity
-cellular stress
-in response to signalling molecules
-deseased vs healthy cells

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3
Q

define the term eukatyote

A

cells which have a clearly defined nucleus

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4
Q

the organelles that have membranes are… (4)

A

-endoplasmic recticulum
-golgi apparatus
-vesicles
-lysosome

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5
Q

description of endoplasmic reticulium

A

-a series of membrane tubules that extend from the nuclear membrane
-rough endoplasmic reticulum: ribosomes dotted along its surface
-smooth endoplasmic reticulium: smooth surface

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6
Q

description of the golgi apparatus

A

a series of flattened membrane disks that proteins pass through to be modified

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7
Q

description of lysosomes

A

-membrane bound organelles that contain hydrolases which are enzymes
-these enzymes break down proteins lipids, nucleic acid and carbohydrates
-hydrolase use water to break the covalent bonds in these substances

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8
Q

description of vesicles

A

membrane protein organelles that transport proteins and other substances around the cell

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9
Q

describe where lipids are synthesised

A

lipids are syrhisised in the smooth endoplasmic reticulum (SER) and inserted into its membrane

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10
Q

whats the difference between cytosol and cytoplasm

A

-cytosol is the fluid in which organelles are suspended
-cytoplasm includes the cytosol and all the organelles (excluding the nucleus) within the plasma membrane

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11
Q

a) describe the synthesis pathway from the nucleus to cytosolic proteins

b) give some examples of cytosolic proteins

A

a) nucleus—>DNA—>gene—>mRNA—>cytosol—>cytostolic ribosome—>protein staying in the cytosol—>cystolic protein

b) protein kinases and CDKs

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12
Q

a) describe the synthesis pathway from the nucleus to trans membrane proteins

b) give some examples of transmembrane proteins

A

a) nucleus—>DNA—>gene—>mRNA—>cytosol—>cytostolic ribosome—>protein attached to the membrane—>transmembrane protein

b) channels, pumps and transporters

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13
Q

a) describe the synthesis pathway from the nucleus to secreted proteins

b) give some examples of secreted proteins

A

a) nucleus—>DNA—>gene—>mRNA—>cytosol—>cytostolic ribosome—>protein leaves the cell—>secreted protein

b)digestive enzyme and peptide hormones

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14
Q

describe the structure of the golgi apparatus

A

the golgi apparatus is a series of flattened membrane disks that proteins can pass through to be modified (post translation modifications)

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15
Q

describe how proteins move through thr golgi apparatus

A

proteins move from one disk to the next in vesicles that bud off and fuse with the next membrane

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16
Q

describe the major post translational modification that occurs in the golgi

A

the addition of carbohydrates to form a glycoprotein

enzymes catalase the addition of various sugars in multiple steps to form carbohydrates

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17
Q

summarise the movement and modification of transmembrane proteins after the insertion of proteins

A

-a transport vesicles carrying a protein leaves the RER membrane & fuses with the golgi

-post translational modification (ie addition of carbohydrate) occurs

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

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18
Q

what is the the string of amino acids that mRNA codes for called and what does it do in the synthesis of transmembrane proteins

A

signal sequence

it determined the final location of the transmembrane protein in the cell

it also prompts the cystolic ribosome to dock with the endoplasmic reticulum

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19
Q

what does the amino acid signal sequence (thats binded to the ribosome) do 2 when it binds to the endoplasmic reticulum in the synthesis of transmembrane proteins

A

directed the ribosome to dock with the ER and stops translation

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20
Q

what does the ER turn into after the ribosome (with signal sequence) has binded and the signal sequence is removed

A

the rough endoplasmic reticulum (translation continues when the signal sequence is removed)

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21
Q

what happens to the signal sequence after it’s been removed from the ribosome

A

the protein (the signal sequence is the protein) is embedded in the RER membrane ready for transport

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22
Q

where are proteins synthesised in the secretory pathway

A

the lumen of the RER

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23
Q

what post post translations do proteins go through in the secretory pathway

A

addition of carbohydrates and proteolytic cleavage

24
Q

once modified what are proteins packaged into in the secretory pathway

A

secretory vesicles

25
Q

what happens in the secretory pathway when the protein is packaged into a secretory vesicle

A

the secretory vesicle travels to the plasma membrane, releasing the protein out of the cells

26
Q

which structure causes a cytosolic ribosome to dock with the ER and also indicated the proteins final location in the cell

A

signal sequence

27
Q

give an example of a secreted protein

A

some digestive enzymes and peptide hormones

28
Q

name the 4 groups attached to the carbon of an amino acid monomer

A

amine group, hydrogen, carboxyl group and R group

29
Q

in what type of reaction do amino monomers join and what type of bond is it

A

condensation and a peptide bond

30
Q

what is a series of amino acid monomers joining to make a amino acid chain called

A

polypeptides

31
Q

how does a poly peptide chain form a protein

A

R group interactions

32
Q

R group classification, acidic-
-hydrophobic or hydrophilic?
-whats the charge
-whats the key component

A

-hydrophilic
-negative
-carboxylic acid group

33
Q

R group classification, basic-
-hydrophobic or hydrophilic?
-whats the charge
-whats the key component

A

-hydrophilic
-positive
-amine group

34
Q

R group classification, polar-
-hydrophobic or hydrophilic?
-whats the charge
-whats the key component

A

-hydrophilic
-neutral
-carbonyl, hydroxyl, amine of sulphdyl group

35
Q

R group classification, non-polar-
-hydrophobic or hydrophilic?
-whats the charge
-whats the key component

A

-hydrophobic
-neutral
-hydrocarbon groups, usually in long chains or rings

36
Q

what is the primary structure of a protein

A

just the polypeptide chair held together by peptide bonds

37
Q

what happens in the secondary structure of a protein

A

hydrogen bonding along the backbone of the protein strand

38
Q

what are the types of secondary structure

A

alpha helices, parallel or anti parallel beta-pleated sheets, or turns

39
Q

what happens in the tertiary structure of a protein

A

the overall shape of the folded protein that is stabilised by R group interactions

40
Q

what are the 5 difference R group interactions

A

-hydrophobic
-london dispersal forces
-ionic bonds
-disulphide bridges
-hydrogen bonds

41
Q

definition of hydrophobic R group interaction

A

when hydrocarbons come close together

42
Q

definition of LDF R group interaction

A

when hydrocarbon groups come together

43
Q

definition of ionic bonds R group interaction

A

electrostatic attraction between oppositely charged ions. can be disrupted by changing the pH or addition of charged molecules. i.e the addition of phosphate

44
Q

definition of disulphide bridge R group interaction

A

strong covalent bond formed between sulphur-containing R groups

45
Q

definition of hydrogen bond R group interaction

A

weak electrostatic attraction between a nearby oxygen or nitrogen atom

46
Q

what is the non protein subunits in a quaternary structure

A

prosthetic groups

47
Q

how does increasing temperature affect protein structure

A

increasing temperature disrupts the interactions that hold the protein in shape. the protein begins to unfold, eventually becoming denatured

48
Q

how does changing pH affect protein structure

A

the charges on acid and basic R groups are effected by pH.

As pH increases or decreases from the optimum the normal ionic interactions between charged groups are lost

which changes the conformation of the protein until it becomes denatured

49
Q

what is the name of the substance that binds to a protein

A

ligands

50
Q

what does a conformation change cause

A

a functional change

51
Q

what effect does a positive modulation have on allosteric enzyme

A

postive modulators increase the enzymes affinity for the substrate

52
Q

what effect does a negative modulation have on allosteric enzyme

A

negative modulators reduce the enzymes affinity for the substrate

53
Q

describe the co-operatively of hemoglobin

A

when and oxygen molecule binds to one of 4 binding sites, this changes the conformation of the remaining 3 binding sites, increasing the affinity of the remaining subunits for oxygen

54
Q

what does a left shift mean on the on the oxygen dissociation curve

A

increased pH and decreased temperature in actively respiring tissue increases affinity of haemoglobin for oxygen

55
Q

what does a right shift mean on the on the oxygen dissociation curve

A

reduced pH and increases temperature in actively respiring tissue reduced affinity of Haemoglobin for oxygen which will reduce the binding of oxygen to haemoglobin, promoting increased oxygen delivery to tissues

56
Q

what is kinase in phosphorylation

A

kinase removes the terminal phosphate group from a molecule of ATP reducing it to ADP (tri phosphate to di phosphate)

kinase then adds that phosphate group to the protein, this changes the conformation and function of that protein

57
Q

what is phosphatase in dephosphorylation

A

phosphate removes the phosphate group from the protein and adds it back onto the ADP regenerating it into ATP

This changes the conformation of a protein back to its original shape

advanced higher biology (7 decks)

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