Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Cell and Molecular > DNA > Flashcards

DNA Flashcards

1
Q

Which are purines and which pyrimidine

A

A and G are purine so 2 rings

T and C are pyrimidine with 1 ring

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What bonds between nucleotides

A

phosphodiester

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is on 5’ end and what on the 3’ end

A

5’ is phosphate

3’ is hydroxyl

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what are the hydrogen bonds between bases

A

C and G = 2

T and A = 1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the hershey case experiment

A

grow virus in 2 different broths one rich in radioactive phosphate(in DNA) one radioactive sulfur (in proteins)
viruses then allowed to infect E.coli and then centrifuged
pellet contains the bacteria, supernatant virus
Bacterial pellet was radioactive with phosphate not sulphur proving that the DNA was inserted by the virus not the protein so the DNA contains the genetic material

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What direction doen DNA polymerase work

A

adds new sugar ti backbone at 3’ end. only synthesises from 5’ to 3’

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What happens to the lagging strand

A

okazaki fragments so not continuous replication. Primers are removed ribonuclease H and polymerase recognises the gaps and fills in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is transcription

A

RNA polymerase binds to primer region and single strand mRNA is synthesised

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what is the role of promoter

A

activity of the promoter determines how much of the protein is produced. It is unidirectional

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Ways to protest mRNA

A

introns spliced out
poly A tail added (AAAAAA)
RNA cap

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the transcriptome

A

section of genome to be transcribed to RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

heterochromatin and euchromatin

A

hetero is inactive transcriptionally dark and dense but euchromatin is loose and active so RNA polymerase gets in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Centromere ?

A

repetive DNA sequence where spindles attach in cell division

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Telomere ?

A

soecialised DNA sequence at ends of linear chromosome that maintain integrity maintained by telomerase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

origin of replication ?

A

where replication starts not at the ends but in the middle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

chemical Mutation

A

EMS and ENU are alkylating agents covalently bind to modify DNA single base pair change

17
Q

Xray mutation cause?

A

induce breakdown of DNA backbone so lose fragments

18
Q

UV mutation cause?

A

causes thymine to covalently bond to each other causing it to be read incorrectly

19
Q

process of translation?

A

tRNA binds to specific complementary codon, peptide bonds form between amino acids that are joint to tRNA on large subunit
stop codon causes release factor to bind, end of peptide

20
Q

role of large and small subunit?

A

large : peptide bond formation

small: decoding mRNA

21
Q

what does the location of the ribosome mean

A

if on ER then it is fro secretion, if free floating it is for local use only

22
Q

what is the N and C terminus?

A

N is with the amine group

C is end with carboxyl

23
Q

how is a peptide bond formed?

A

a condensation reaction, catalysed by peptide transferase

24
Q

What affect does urea have on protein?

A

denatures it, if removed it reverts back

25
Q

What is the quaternary structure?

A

when 2 subunits bind to form a dimer, can be identical - homotetramer or different: heterotetramer

26
Q

Type one and type 2 transmembrane protein difference?

A

1; has N terminus extracellular

2: N terminus intracellular

27
Q

What are lipid modifications?

A

covalently attached lipid t help protein bind. Intracellular = acylation and prenylation
Extracellular = GPI anchor

28
Q

Role of glycosylation?

A

provides sticky surface, adhesive properties sugar can bind to amino acids

29
Q

Phosphorylation role?

A

kinases catalyse, need ATP, gives a negative charge

30
Q

How is GTP activated and inactivated

A

by adding and losing a phosphate

31
Q

What is an SRP used for?

A

ensuring the protein goes to the correct destination. the receptor is complementary to the signal sequence in the amino acid chain

32
Q

Steps in protein modification when at ER

A
  1. arrives at ER lumen,directed by the signal sequence to the SRP
  2. once bound SRP released and recycled
  3. ribosome and protein are at a translator channel and it opens
  4. protein fed through and signal sequence is cleaved off
33
Q

What is the role of a chaperone?

A

ensure the proteins fold correctly as bind to the hydroponic regions that are visible and shouldn’t be and cause hydrolysed to result in change in folding

34
Q

2 types of chaperone and differenced

A

Hsp60 - when already folded but wrong, enters a chamber that is then capped and ATP needed
Hsp70 - used when it is actively folding

35
Q

What if still not folding after chaperone?

A

targetted and tagged which ubiquitin, causes it to be degraded in proteasome and cleaved into peptides

Cell and Molecular (12 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions