Protein Structure And Synthesis Flashcards

1
Q

What are proteins?

A

Proteins are linear chains of amino acids arranged in a 3D structural hierarchy

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2
Q

What are intrinsically disordered proteins (IDS)?

A

Proteins that have lost their native, functional folding resulting in insoluble aggression in many organs.
Causing many diseases

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3
Q

Structure of amino acids

A

Carbon, an amino group and a carbonyl functional group

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4
Q

How are amino acids bonded to form proteins?

A

Linked by covalent peptide bonds formed between carboxylic acid and amino groups of two consecutive amino acids.

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5
Q

How are amino acids bonded to form polypeptides?

A

Continuous peptide bonds between amino acids form polypeptides and the backbone of the protein.

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6
Q

What are the 4 levels of protein structures?

A

Primary
Secondary
Tertiary
Quaternary

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7
Q

What is a primary level of protein structure?

A

Unique sequence of amino acids in a polypeptide chain, with no folding.

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8
Q

What is the secondary level protein structure?

A

Stable special coils and folds of segments within a polypeptide chain.
Forms H-bond between backbone amino and carbonyl groups.

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9
Q

What is the tertiary level protein structure?

A

Three dimensional folding pattern determined by interactions among various side chains.
Stabilised by hydrophobic interactions, ionic bonds and hydrogen bonds.

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10
Q

What is the quaternary level protein structure?

A

Two or more polypeptide chain closely packed arrangement.

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11
Q

What changes in transcription?

A

DNA to mRNA

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12
Q

Why does transcription happen in the nucleus?

A

DNA is too large to leave the nucleus.

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13
Q

How do we produce pre-messenger RNA?

A

RNA polymerase uses one of the DNA strands as a template to produce pre-messenger RNA, which codes for proteins.

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14
Q

What are the 3 phases of transcription?

A

Initiation
Elongation
Termination

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15
Q

When does RNA processing occur?

A

Before pre-messenger RNA can leave to the cytosol.
Polyadenylation at 3’ end
Splices ( exons are joined together)

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16
Q

What changes in translation?

A

RNA to protein in the cytoplasm on the ribosomes.

17
Q

What are tRNAs?

A

Adapters between codons of mRNA and the corresponding amino acid.
Ensures that the genetic code is applied.

18
Q

What happens during initiation?

A

Ribosome gets together with the mRNA and the first tRNA.

19
Q

What happens during elongation?

A

Amino acids are linked to form a chain.

20
Q

What happens during termination?

A

Finished polypeptide is released.

21
Q

how many hydrogen bonds are between a C-G pair?

A

3

22
Q

how many hydrogen bonds are between a A-T pair?

A

2

23
Q

which enzyme is responsible for denaturing DNA strands during genome replication?

A

helicase

24
Q

what monomers are used to produce pre-mRNAs?

A

ribonucleotides

25
Q

what monomers are used to produce proteins in translation?

A

amino acids

26
Q

where does transcription happen?

A

nucleus

27
Q

where does translation happen?

A

cytoplasm

28
Q

what type of bond is formed between ribonucleotides?

A

phophodiester bonds

29
Q

what type of bond is formed between amino acids?

A

peptide bonds

30
Q

in what direction does the new polymer form in transcription?

A

5’ –> 3’

31
Q

in what direction does the new polymer form in translation?

A

n-term –> c term

32
Q

what is the difference between peptide and a protein?

A

peptide has less than 50 amino acids

33
Q

which type of RNA contains the codon?

A

mRNA

34
Q

which type of RNA contains the anticodon?

A

tRNA

35
Q

which type of RNA carries the amino acids to the mRNA?

A

tRNA

36
Q

which type of RNA is involved in the formation of ribosomal subunits?

A

rRNA

37
Q

which region of the primary transcript is removed in the splicing reactions?

A

introns