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?

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
How does cisplatin work?
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
What does society need to do when it comes to cisplatin?
Assess the balance between the benefits and the adverse effects of drugs, like cisplatin.
27
How can you counter the adverse effects of cisplatin?
Use very small amounts or target the drug specifically to cancer cells.
28
Why does cisplatin have adverse effects?
It can kill healthy, normal cells by binding to the DNA in those cells and stopping replication.
29
How does cisplatin prevent DNA replication?
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.