O2: 30 Amino acids, proteins, and DNA Flashcards

1
Q

What properties do amino acids have?

A

Both acidic and basic.

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2
Q

How do you draw a zwitterion?

A

NH2 -> NH3+
COOH -> COO-

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3
Q

How do you draw an amino acid in acidic conditions?

A

NH2 -> NH3+

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4
Q

How do you draw an amino acid in alkaline conditions?

A

COOH -> COO-

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5
Q

What are proteins?

A

Sequences of amino acids joined by peptide links.

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6
Q

Explain the importance of hydrogen bonding and sulfur-sulfur bonds in proteins.

A

Hydrogen bonds exist between polar groups, stabilising the secondary and tertiary structures of proteins.
Disulfide bonds link together and stabilise the tertiary structure.

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7
Q

What is the primary structure of proteins?

A

The sequence of amino acids.

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8
Q

What is the secondary structure of proteins?

A

Hydrogen bonds form between peptide links, folding the protein into either an a-helix or B-pleated sheet.

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9
Q

What is the tertiary structure of proteins?

A

More bonds form between groups in the protein.
e.g. hydrogen bonds, disulfide bridges, ionic bonds.

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10
Q

What does hydrolysis of the peptide link of a protein produce?

A

The constituent amino acids.

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11
Q

How can amino acids be seperated and identified?

A

By thin-layer chromatography.

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12
Q

How can amino acids be located on a chromatogram?

A

Using developing agents like ninhydrin or UV light.

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13
Q

How can amino acids be identified on a chromatogram?

A

By their Rf values.

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14
Q

Draw a peptide bond.

A

H-N=C-O

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15
Q

What is the formula for Rf values?

A

Rf value = distance travelled by spot / distance travelled by solvent

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16
Q

What are enzymes?

A

Proteins.

17
Q

Explain the ‘lock and key’ model for enzymes.

A

Enzymes’ active sites are highly specific so the substrate needs to have a complementary shape in order for the reaction to be catalysed.

18
Q

Explain stereospecificity in enzymes.

A

Because enzymes’ active sites are so highly specific, only one enantiomer of the substrate will work. Enzymes are proteins so also contain chiral centres.

19
Q

How can drugs work as enzyme inhibitors?

A

The drugs have a similar shape to the substrate so they bind to the active site, blocking it from substrate molecules.

20
Q

How are drugs designed now?

A

With the help of computers to model enzymes’ active sites and predict how drugs will interact with them.

21
Q

What is a nucleotide made up from?

A

A phosphate ion bonded to 2-deoxyribose which is bonded to a base.

22
Q

What is the structure of a single strand of DNA?

A

A polymer of nucleotides linked by covalent bonds between the phosphate group of one nucleotide and the 2-deoxyribose of another.
This results in a sugar-phosphate polymer chain with bases attached to the sugars.

23
Q

What does DNA exist as?

A

Two complementary strands arranged in the form of a double helix.

24
Q

What is cisplatin used as?

A

An anticancer drug.

25
Q

How does cisplatin work?

A

It prevents DNA replication in cancer cells by a ligand replacement reaction with DNA.
A bond is formed between platinum and a nitrogen atom on guanine.

26
Q

What does society need to do when it comes to cisplatin?

A

Assess the balance between the benefits and the adverse effects of drugs, like cisplatin.

27
Q

How can you counter the adverse effects of cisplatin?

A

Use very small amounts or target the drug specifically to cancer cells.

28
Q

Why does cisplatin have adverse effects?

A

It can kill healthy, normal cells by binding to the DNA in those cells and stopping replication.

29
Q

How does cisplatin prevent DNA replication?

A

The N atoms on guanine form co-ordinate bonds with cisplatin’s platinum, replacing the chlorine ligands in a ligand substitution reaction.
This causes the DNA strands to kink so they can’t unwind and replicate properly.