Amino Acids and DNA A2 Flashcards

1
Q

What’s the functional group of amino acids

A

Carboxylic acid and primary amine

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2
Q

What are zwitterions

A

Ions that have a permanent positive and negative charge, but is overall neutral

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3
Q

What occurs when amino acids are placed with something highly acidic

A

The lone pair at the amine accepts a H+ ion, forming a positive ions

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4
Q

What occurs when amino acids are placed with something highly alkaline

A

The -OH loses a proton to form a negative ion

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5
Q

What occurs when two amino acids react

A

Forms an amide linkage -CONH-. This is a peptide

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6
Q

What are proteins

A

Molecules containing more than 50 amino acids, forming a polypeptide

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7
Q

What is the primary structure of a protein

A

A fixed sequence of amino acids for each particular protein

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8
Q

What occurs when polypeptides are boiled with HCl calatyst

A

All the original amino acids are reformed as the bonds are hydrolysed

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9
Q

What is the secondary structure of a protein

A

Forms either a helix or a pleated sheet structure, held together by hydrogen bonds or sulfur-sulfur bonds

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10
Q

Where do sulfur-sulfur bonds come from

A

Amino acids like cysteine has sulfur side chain which can bond the sulfurs together

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11
Q

What is the tertiary structure of a protein

A

The alpha-helix or beta-pleating sheet can itself be folded into 3 dimensions, containing hydrogen bonds, sulfur-sulfur bonds and ionic interactions

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12
Q

How can the structure of a protein be identified

A

Reflux with 6 moldm-3 HCl to hydrolyse the protein into amino acids, forming a mixture. This is then used on thin-layer chromatography

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13
Q

Describe thin-layer chromatography

A

Mixture of amino acids are placed on a starting line and a solvent is placed 0.5cm below the starting line. After some time, the solvent will go up pulling each amino acids at different rates, depending on the affinity for their stationary phase

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14
Q

What is done to the amino acids at the end of thin-layer chromatography

A

Developing agents are sprayed on the plate such as ninhydrin (or UV) to form a purple compound. The amino acids will be separated

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15
Q

How to calculate Rf

A

Distance moved by spot / Distance moved by solvent

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16
Q

What are enzymes

A

Protein-based catalysts, optimised for just one reaction

17
Q

Describe the shape of an enzyme

A

They have a crevice called the active site, where the catalysis takes place

18
Q

What does stereospecificity mean

A

The active site of an enzyme is so specific that it can catalyst only one of a pair of enantiomers

19
Q

How to stop an enzyme’s power to catalyse

A

Enzyme inhibition where a molecule similar to the shape of the substrate is produced, taking its spot. Penicillin does this

20
Q

How are drugs produced to cause enzyme inhibition

A

Using computers to analyse long protein chains

21
Q

What are nucleotides

A

Monomers which make up the DNA

22
Q

What makes up a nucleotide

A

Phosphate group, bonded with the sugar 2-deoxyribose and one of the four organic bases

23
Q

Describe the full structure of DNA

A

DNA exists as two complementary strands arranged in the form of a double helix, via hydrogen bonds

24
Q

What is the example of an anti-cancer drug

A

Cisplatin, with the formula Pt(Cl)2(NH3)2

25
Q

How does cisplatin work

A

They bond to strands of DNA, distorts their shape and stop replication of cells. A dative bond is formed between platinum and a nitrogen atom on guanine

26
Q

What are the issues with cisplatin

A

They can stop the replication of healthy cells like hair cells