generating diversity Flashcards

1
Q

what is the priamry structure of a protein?

A

the sequence of amino acid that codes for a gene

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2
Q

what is the secondary structure of a protein?

A

folds of amino acid sequence to make alpha helices and beta pleated sheets

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3
Q

what is the tertiary structure of a protein?

A

overall 3D shape

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4
Q

what do alpha helices allow?

A

proteins able to insert into a membrane

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5
Q

beta pleated sheets

A

bonds that make up beta sheets are incredibly weak, however there are many of them, making it stronger
aggregation by beta pleated sheets with neurogenerative disorders

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6
Q

what is the quaternary structure of a protein?

A

multi-subunit assembly

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7
Q

the process of gene mutations result in…

A

related proteins with altered function

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8
Q

what does a point mutations result in?

A

altered primary sequence (e.g A swapped with G) by changing one nucleotide to a different one
effects= silence, misense and nonsense

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9
Q

how does insertion result in an altered primary sequence?

A

new nucleotides inserted resulting in different gene

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10
Q

how does deletion result in an altered primary sequence?

A

removes nucleotides resulting in a frame shift

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11
Q

gene duplication resulting in new proteins

A

not initially translated due to stop codon however if a poit mutation/deletion occurs in stop codon then there will be two copies of a single gene

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12
Q

what channels evolved by gene duplication?

A

sodium (duplicated 4 times) and calcium ion channels

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13
Q

relation of metabotropic glutatmate receptors

A

phyligenetic relation of G-protein coupled receptors fall into 3 groups that are dependent on sequence similarity and act ia different signalling mechanisms

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14
Q

group 1 of G-protein coupled receptors

A

mGluR1 and mGluR5

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15
Q

group 2 of G-protein coupled receptors

A

mGluR2 and mGluR3

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16
Q

group 3 of G-protein coupled receptors

A

mGluR7, mGluR4, mGluR8 and mGluR6

17
Q

how many receptors are in the GPCR superfamily?

A

> 1200 receptors

18
Q

quaternary structure adn ion channels

A

multiple individual proteins (monomers)
combine to form a ‘super-protein’ (multimer)
ion channels are multimeric assemblies

19
Q

nAChR (nicotinic acteylcholine receptor) subunits?

20
Q

NMDAR (glutamate receptors) subunits?

21
Q

subunit composition

A

1=1
2=6
3=21
number of possible combinations increases with the number of available subunits and number of subunits required

22
Q

GABAa receptor subunit composition

A

1000s of possible receptors from 13 genes but only a small number detected

23
Q

alternative splicing

A

exon splicing can be variable e.g via exon skipping, creating splice variants (diffrential splicing)

24
Q

alternative/diffrential splicing in the D2 dopamine receptors

A

there are 6 exons in the D2 receptors however sometimes exon 5 is not spliced

25
Q

difference between D2 receptors

A

D2 (short) receptor is a pre-synaptic autoreceptor whereas D2 (long) receptor is post-synaptic
this is determined by a 29 amino acid insert in the long receptor

26
Q

alternative splicing effects

A

has been found to be ubiquitous in eukaryotic cells (every single gene expressed is expressed in multiple ways)
e.g. in humans, ~95% of multiexonic genes may be alternatively spliced
DSCAM homologue from drosophila melanogaster (fruit fly) could have as many as 38,000 splice variants and it only has 15,000 genes

27
Q

RNA editing (adenosine)

A

when you deaminate adenosine you create inosine, which is recognised by tRNA as guanosine

28
Q

RNA editing explanation

A

enzymatic, post-transcriptional modification of RNA
most common form in eukaryotic cells is conversion of adenosine to inosine
results in codon change and so a change in protein 1o
sequence