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biochem > biochem MQ > Flashcards

biochem MQ Flashcards

1
Q

How many chromsomes do humans have

A

23 pairs of chromosomes

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2
Q

what are condensed regions of DNA called?

A

Heterochromatin

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3
Q

what did Treptococcus, Griffith and colleagues prove?

A

That bacteria can transfer genetic materail

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4
Q

What is the bacteriophage labelled with in the Hershey-Chase experiment

A

Sulfure-35

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5
Q

Does the number of chromosomes correlate with the complexity of an organism

A

No

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6
Q

Does the BCR-Abl fusion protein arise from chromosomal translocation

A

yes

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7
Q

does sickle-cell diease arise from a single nucleotide change in the alpha-globin gene

A

no

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8
Q

In the avery experiment did the DNAase treatment of heat killed smooth strain material result in transfromation of rough strain

A

No

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9
Q

Do mutations in the CFTR gene affect calcuim balance in the airway epitheluim

A

No

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10
Q

Why is the smooth strain of Streptococcus deadly to mice

A

Due to the ability to evade the host immune system

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11
Q

What purine base is contained within DNA

A

Adenine

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12
Q

What carbon of deoxyribose is the primary alcohol on

A

5

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13
Q

What properties of DNA did Rosalind Franklin and Maurice whilkins provide via their x-ray diffraction

A

double helix
phsphates on the oustide

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14
Q

What effect does high salt have on DNA melting

A

Increases melting temperature by neutralising negatively charged phosphate backbone

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15
Q

Is B-DNA is a right handed- helix

A

yes

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16
Q

What type of handed helix is Z-DNA

A

left

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17
Q

If the conservative model of replication would have been proven by Meselson and Stahl , what woudl you expected at the 1st generation

A

50% at the 14N density , 50% at the 15N density

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18
Q

What is the primary reason for the use of a DNA polymerase , such as Taq for PCR

A

Due to its ability to withstand high DNA denaturing temperatures

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19
Q

What is required for next generation sequencing?

A

Polymerase chain reaction
Nucleotides with a 3’ reversible blocking group

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20
Q

what subunit stabilises the assembled E.Coli RNA polymerase

A

omega

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21
Q

What subunit directs the E.Coli RNA polymerase to the correct trasncription initaion sites?

A

sigma

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22
Q

Where are the signals for termination

A

in the newly synthesised RNA

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23
Q

What does the poly A tail do

A

Increases stability and assits in nuclear export

24
Q

What does the 5’cap added to MRNAS in eukaryotes contain?

A

7-methyl-cytidine

25
Q

What is the splicesome comprised of

A

protein and snRNA

26
Q

What do miRNAS do and whats their aim

A

miRNAS destabilise mRNAS eitjer leading to their degradation or blocking translation , the aim is to block protein production

27
Q

What did Avery prove about DNA

A

Proved that DNA caused the transformation

28
Q

How many hydrogen bonds between pairs AandT and GandC

A

A-T=2
G-C=3

29
Q

What are the histones in chromatin?

A

H1,H2A,H2B,H3,H4

30
Q

What is the role of H1 histone

A

its a linker histone and helps compact DNA

31
Q

What tells the polymerase when to stop?

A

Termination signals

32
Q

what enhances and blocks promotors?

A

enhance-activators
block-supressors

33
Q

What is an operon

A

A group of genes that are trasncribed together to produce a single messenger RNA molecule that encodes multiple proteins

34
Q

What are genes called that are expressed all of the time

A

constitutive expression

35
Q

what are genes called that are expressed under certain conditions

A

regulated expression

36
Q

What does allolactose do?

A

Binds to the repressor and prevents it from binding to the operator so that the gene can be transcribed

37
Q

what is an operator

A

an operator is a DNA sequence that controls the transcription of genes by binding to regulatory proteins

38
Q

What does microRNA do

A

Bind to specific mRNA and leads to degradation of mRNA

39
Q

What are the characteristics of fibrous proteins?

A

insoluble , silk-web, intracellular cytoskeleton, extracullar matrix

40
Q

what are the charactertics of globular proteins?

A

soluble, exact 3d shape is critical in their fucntion

41
Q

how many different side chains are used in proteins?

A

20

42
Q

what are the 20 different amino acids?

A

glycine
alanine
cysteine
phenylalanine
methionine
tryptophan
valine
leucine
isoleucine
proline
serine
threonine
asparagine
glutamine
tyrosine
aspartic acid
glutamic acid
lysine
arginine
histidine

43
Q

what are the non polar amino acids

A

glycine
alanine
valine
cysteine
proline
leucine
isoleucine
methionine
tryptophan
phenylalanine

44
Q

whta are the amino acids with a positive charge

A

lysine
arginine
histidine

45
Q

what are polar amino acids?

A

serine
threonine
tyrosine
asparagine
glutamine

46
Q

What are the amino acids with a negative charge

A

aspartic acid
glutamic acid

47
Q

why do non-polar groups like to cluster together?

A

Because of their inability to form H-bonds , they group together because of a need to avoid water

48
Q

What did Brenner and Crick suggest?

A

suggested that each codon must contain three bases

49
Q

Where do release factors bind to

A

They bind to the A site

50
Q

what three stages is translation divided into

A

initiation
elongation
termination

51
Q

What did Linus Pauling and Robert Corey try to do?

A

They tried to work out the structure of the fibrous protein a-keratin using X-ray diffraction data

52
Q

What three rules did they have to follow to fit the data?

A

1-there can be no rotation aroudn the planar peptide bonds
2-other parts of the chain must be felxible
3-structure must have the maximum number of stabilising forces between residues and stabilising forces must be indepdent of primary structure

53
Q

why is the anti parallel beta sheet more stable than parallel

A

Ati -parallel is more stable as it contains more H-bonds and the H-bond atoms are aligned directly opposite making for stronger bonds

54
Q

what is calmodulin

A

calmodulin is a protein that binds to calcium and regulates processes

55
Q

how many calcuim binding sites does calmodulin have and how many different proteins can it bind to?

A

4 calcuim binding sites
can bind to two different proteins

56
Q

How does calmodulin activate a protein

A

biochem (3 decks)

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