Collinearity of gene and protein Flashcards

1
Q

How many groups of amino acids are there

A
FOUR
9 hydrophobic
6 hydrophilic
2 negatively charged
3 positively charged
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2
Q

What is the importance of R group

A

Interactions between R groups determine shape of protein and if it’s functional
Reacts with substrate

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3
Q

How do amino acids join

A

Join unbranched polypeptides via condensation reactiom

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4
Q

What is a tetramer and an example

A

Haemoglobin, made of four polypeptide chains

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5
Q

What causes sickle cell anaemia

A

Gene defect heterozygous half beta chains altered and half normal - still suffer as a tetramer so only 1/4 haemoglobin is functional

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6
Q

What is a repressible operon

A

Turn off anabolic path when end product available

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7
Q

When is the trp operon in process

A

When tryptophan is present

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8
Q

What is the product of trpR

A

aporepressor protein

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9
Q

What does the aporepressor need to bind to the operator

A

Needs tryptophan in medium to bind to it to activate it

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10
Q

What happens when the aporepressor binds to the operator

A

Stops transcription of trp operon

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11
Q

When is trp operon triggered

A

Low/no tryptophan present

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12
Q

What does attenuation do

A

Prevents the completion of transcription of trp operon

mechanism to prevent trp transcription when levels are high

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13
Q

What causes more short transcripts

A

High amount of tryptophan in cell

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