Biochem Flashcards

1
Q

What is the difference between a nucleotide and a nucleoside?

A
Nucleotide = base + sugar + phosphate
Nucleoside = base + sugar
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2
Q

What end are new nucleotides added on to and what direction is DNA read in?

A

New nucleotides added to 3’ end

Read from 5’ - 3’

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3
Q

What type of bond is between A and T and C and G?

A

A=T (double bond)

C=-G (triple bond)

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4
Q

What enzyme catalyses DNA replication?

A

DNA polymerase (can only build onto an RNA primer - primase)

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5
Q

Where does DNA transcription start and which side does it read?

A

Origins or replication (there are multiple points)

Bidirectional

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6
Q

What are the 2 strands called in DNA replication?

A
Leading strand (has a free 3' end)
Lagging strand (okazaki fragments)
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7
Q

What enzyme unwinds DNA?

A

Helicase

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8
Q

What enzyme checks the transcribed DNA strand for mutations?

A

DNA polymerase

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9
Q

Where on DNA is the initiation site for RNA transcription?

A

Promotors - TATA box

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10
Q

Where are steroid receptors active?

A

Only in the nucleus (inactive in the cytoplasm)

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11
Q

What are the 3 tRNA binding sites on a ribosome?

A

EPA
E = exit
P = peptidyl
A = aminoacyl

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12
Q

What are the types of chomosomal mutation?

A

Deletion,
Duplication,
Translocation,
Inversion

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13
Q

What are the types of DNA mutation?

A

Point, frameshift

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14
Q

What is the difference between lock-and-key enzyme binding and induced fit?

A

Lock and key: active site of substrate is complementary to that of the enzyme
Induced fit: partial binding of the enzyme initiates a conformational change which increases binding of the enzyme to the substrate

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15
Q

What enzyme phosphorylates and what dephosphorylates a molecule?

A

Phosphatase: dephosphorylates
Kinase: phosphorylates

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16
Q

What is Km?

A

The concentration of substrate and which the reaction is progressing at half of Vmax

17
Q

On a line weaver-Burk plot which point indicates Km and which indicates Vmax?

A

Km: intersection with X axis (1/[S])
Vmax: intersection with y axis (1/v)

18
Q

What does a low Km indicate?

A

Higher affinity for the substrate (needs a lower conc to progress at a high rate)

19
Q

What is the difference between competitive and non-competitive inhibition and are they reversible?

A

Competitive: inhibitor binds to same site as substrate to stop it binding
Non-competitive: inhibitor binds to site other than substrate and changes the conformation of the active site to prevent binding
Both are reversible

20
Q

In competitive and non-competitive inhibition which factor remains constant?

A

Competitive: Vmax remains constant (Km varies)

Non-competitive: Km remains constant (Vmax varies)