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AH Biology > Unit 1 KA2 > Flashcards

Unit 1 KA2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the proteome?

A

It is all the proteins made from all the genome

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2
Q

In eukaryotic cells, what size is the proteome compared to the genome. (2 points) Why? (3 points)

A
  1. Larger
  2. Because alternative RNA splicing allows for more than one protein to be expressed
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3
Q

Not all genes are expressed as…

A

Proteins in a particular cell type

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4
Q

What can happen to the set of proteins expressed over time?

A

They can vary because of certain conditions

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5
Q

Name the factors that can affect types of proteins expressed

A
  1. Metabolic activity
  2. Cellular stress
  3. Response to signalling molecules
  4. Disease
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6
Q

Give an example of metabolic activity

A

Age
Dormancy state

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7
Q

Give an example of cellular stress

A

Extremes of:
- temperature
- pH
-exposure of toxins

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8
Q

Give an example of a response to signalling molecules

A

Hormones

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9
Q

What can RNA genes be transcribed to produce?

A

tRNA, rRNA, mRNA, RNA molecules that
1. Control gene expression of other genes
2. Protection of telomeres

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10
Q

Alternative RNA Splicing

definition

A

Removal of non-coding introns from a primary mRNA transcript to leave only the coding exons; several different mature transcripts can be produced from a single primary transcript

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11
Q

ER

what does it stand for and what is the definition?

A
  1. endplasmic reticulum
  2. a network of membrane tubules within the cytoplasm of a eukaryotic cell, continuous with the nuclear membrane
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12
Q

exon

definition

A

a section of RNA that is usually retained in splicing

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13
Q

Glycoprotein

definition

A

a protein with a carbohydrate added by post-translational-modification

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14
Q

Golgi Apparatus

how is it identifiable? definition.

A
  1. it is a series of membrane discs
  2. it packages proteins into membrane bound vesicles inside the cell before the vesicles are sent to their destination

looks like pancakes, acts as the amazon of the cell

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15
Q

Hydrolases

A

a class of enzymes that use water the break chemical bonds

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16
Q

intron

A

a section of RNA that is usually removed during splicing

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17
Q

Lysosome

definition

A

a modified golgi vesicle containing hyrolytic enzymes

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18
Q

Non-coding RNA gene

A

A gene that codes for RNAs other than mRNA so do not code for a protein

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19
Q

phospholipid

definition

A

component of cell membranes

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20
Q

post-translational modification

definition

A

addition of different chemical groups to, or modification of, a protein to allow a particular function

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21
Q

Proteolytic cleavage

definition

A

A major form of post-translational modification
digestive enzymes require this
activate protein

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22
Q

Proteolytic cleavage

process in brief and the purpose of this

A

occurs when a protein cleaves one or more bonds in a target protein to activate, inhibit or destroy the protein’s activity

cleaves- cuts out

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23
Q

RER

definition

A
  1. Rough endoplasmic reticulum
  2. organelle made up of membranes with ribosomes attached
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24
Q

Signal sequence

A

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

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25
Q

SER

what it stands for and definition

A
  1. Smooth endoplasmic reticulum
  2. an organelle found in most eukaryotic cells
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26
Q

what does SER produce compared to RER

A

SER- lipids, steroid hormones
RER- proteins

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27
Q

vesicles

definition

A

small membrane bound compartments filled with liquid

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28
Q

microtubules

definition

A

a network of tubes where vesicles move across the cell

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29
Q

cytosolic proteins

definition

A

finish translation in cytosol and stay there to synthesise proteins
carry a signal sequence that directs them to the correct location inthe cell

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30
Q

cytosolic proteins

examples

A

enzymes of glycolisis
enzymes that attach amino acids to tRNA molecules for use in protein synthesis

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31
Q

where does ALL protein synthesis start?

A

cytosol

32
Q

transmembrane protein production

steps

A
  1. begins in cytosolic ribosomes
  2. signal sequence causes CR to dock with ER forming RER
  3. translation is halted
  4. transmembrane protein is synthesised
  5. once translation is completed ribosome is released back into cytosol
  6. proteins that are in the ER are transported by vesicles and fuse with thegolgi apparatus
33
Q

what happens to the vesicles after transmembrane protein production

A

they go through the golgi apparatus where they undergo post translational modification

34
Q

after the vesicles leave the golgi what happens

how is this done?

A

they take they proteins to the plasma membrane and lysosomes
they move along microtubules

35
Q

sectretory pathway

steps

A
  1. secreted proteins are translated in ribosomes on the RER and enter its lumen
  2. proteins move through the golgi and then are packaged into sectretory vesicles
  3. these vesicles move to and fuse with the plasma membrane
  4. this releases the proteins out of the cell
36
Q

proteolytic cleavage

steps

A

inactive protein has its masking sequece cleaved to produce an active enzyme

37
Q

4 types of amino acid groups

A
  1. basic (+ve)
  2. acidic (-ve)
  3. polar
  4. hydrophobic
38
Q

what does the R group do to the amino acid

A

it gives unique chemical propities and specific shape

39
Q

basic amino acid

how many and how are they uniquely identifiable?

A
  1. 3
  2. have NH2 on the R GROUP

they are strongly hydrophilic

40
Q

acidic amino acid

how many are there and how are they made uniquely identifiable?

A
  1. 2
  2. they have a carboxylic group on the R group

they are strongly hydrophobic

41
Q

polar amino acids

how are they identifiable?

A

they either have N, O, S on their side chain
also may include hydorxyl, carbonyl and amine group

42
Q

hydrophobic (non-polar) amino acid

how are they identifiable?

A

they have long R chains with H on them

nothing special about them and have no charge

43
Q

What is the primary structure of proteins?

SQA definition

A

sequence in which the amino acids are synthesised into the polypeptide

44
Q

What is the secondary structure of proteins?

SQA definition

A

hydrogen bonding along the backbone of the protein strand results in regions of secondary structure

45
Q

What are the 3 types of secondary structure in proteins?

A
  • Alpha-helices
  • parallel/antiparallel beta-pleated sheets
  • turns
46
Q

How can secondary protein structures be identified?

their features

A
  • Alpha-helices = spirals
  • Beta-pleated sheets = zigzags or corregated material
  • Turns = a point in which the polypeptides reverses or changes direction
47
Q

What types of interactions hold the R groups in the tirtery structure together?

A
  • Hydrophobic interations
  • ionic bonds
  • hydrogen bonds
  • LDFs
  • Van der Waals interactions
  • Disulfide bridges
48
Q

What is the quaternary protein structure?

A

It exists in proteins with several connected polypeptide subunits held together by the interations seen in the tirtary groups

49
Q

What is a prosthetic group?

Give an example

A
  • they are a non-protein structure that are necessary for its function
  • example of haem on haemoglobin
50
Q

What are the two factors that affect protein structure?

A
  • pH
  • temperature
51
Q

When changing the factors that affect protein structure, what specifically happens to bonding and interactions?

include both factors in your answer

A
  • An increase in temperature will disrupt weaker bonds and possibly melt covalent ones
  • A change in pH will result in the normal ionic interations between R groups being lost.
52
Q

What is the name given to the ends of the secondary structure?

A

c terminus and n terminus

53
Q

What is a ligand?

A

a substance that can bind to a protein

54
Q

What allows binding to ligands?

A

R groups

55
Q

What does protein folding produce?

A

ligand binding sites on the surface of the protein

56
Q

what is a nucleosome?

A

combination of DNA being wrapped around histone protein

57
Q

What is a ligand?

A

a substance that can bind to a protein

58
Q

What does protein folding produce?

A

ligand binding sites that will have complementary shape to the ligand

59
Q

Nucleosome

A

DNA is wrapped around histones to form this

60
Q

What changes when the ligand binds to a protein binding site?

A

conformation of protein which therefore changes function of protein

61
Q

What does the binding of one molecule do to one active site of an allosteric enzyme?

A

it increases the affinity of the other active sites for binding of subsequent substrate molecules

62
Q

In binding what do many allosteric enzymes show?

A

co-operativity

63
Q

What is co-operativity?

A

changes in binding at one subunit alter the affinity of the remaining subunits

64
Q

What are allosteric enzymes?

A

enzymes that contain an allosteric site (non-substrate binding site)

65
Q

What are modulators?

A

they are examples of ligands

66
Q

What do modulators do?

A

regulate the activity of the enzyme when they bind to the allosteric site

67
Q

What happens after the binding of a modulator to the allosteric site?

A

the conformation od the enzyme changes which alters the affinity of the active site for the substrate

68
Q

What do + and - modulators do?

A

+ increase the affinity of the enzyme to the substrate +
- decrease the affinity of the enzyme to the substrate -

69
Q

Give an example of cooperativity

A

release of oxygen in haemaglobin- changes the binding of oxygen at one subunit alters the affinity of the remaining subunits for oxygen

70
Q

What affect the binding of oxygen to haemaglobin

A
  • pH
  • temperature
71
Q

how do the factors lower the affinity of haemaglobin for oxygen?

A

a decrease of pH (from the production of carbonic acid)
an increase in temperature

this means when your body is hot oxygen can be released into your blood

72
Q

how do factors increase the affinity of haemaglobin for oxygen?

A

increase in pH
decrease in temperature

reduces oxygen delivery to tissue

73
Q

What can cause reversible conformational change in proteins?

A

The addition or removal of phosphate

74
Q

what is phosphorilation?

A

a common form of post transational modification

75
Q

what do protein kinases do?

A

catalyse the transfer of a phosphate group to other proteins

add to

76
Q

What do protein phosphatases do?

A

catalyse the removal of phosphate from a protein

take away

77
Q

Phosphorylation

A
  • can activate or inhibit proteins
  • brings about conformational change that can affect te proteins activity
  • adding a phosphate group creates a negative charge
  • activity of cellular proteins can be regulated by phosphorylation

AH Biology (2 decks)

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