3.13 Amino acids, proteins and DNA Flashcards

1
Q

What are the 2 functional groups of amino acids

A

NH2 and COOH (amine and carboxylic acid)

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2
Q

Draw a general formula for alpha amino acids

A

google

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3
Q

Are alpha amino acids chiral, why

A

Yes one carbon has 4 different substituents
Except glycine where R=H

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4
Q

In what form do amino acids exist as solids
What consequence does this have

A

Zwitterions (ionic lattice) - high mtp and bpt

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5
Q

What colour solids are most zwitterions at room temp

A

White solids

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6
Q

Do zwitterions dissolve in water? Non polar solvents? Why?

A

Yes, but only in non polar solvents. Due to ionic nature/polar bonds

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7
Q

Define a zwitterion

A

Ions which have both a permanent positive and negative charge, but are neutral overall

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8
Q

How do zwitterions occur in amino acids? Draw a general structure of one

A

COOH is deprotonated –> COO-
NH2 is protonated –> NH3+

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9
Q

What happens to amino acids in acidic conditions

A

Gains a proton on NH2 group

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10
Q

What happens to amino acids in alkaline conditions

A

Loses a proton from COOH group

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11
Q

What is the peptide linkage

A

-CONH-
The peptide linkage

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12
Q

What is a dipeptide

A

2 amino acids bonded together

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13
Q

What is a TLC plate made of

A

Plastic sheet coated with silica, SiO2
This is the stationary phase (the solvent is the mobile phase)

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14
Q

Describe how you would carry out TLC

A

Spot the samples onto a pencil line a few cm above base of TLC plate
Place this in a beaker or tank, with solvent level below the pencil line. Ensure there is a lid of the beaker to keep the inside saturated with solvent vapour
Wait until the solvent front is almost at the top of the TLC plate; then remove from the beaker and analyse

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15
Q

Why does TLC separate amino acids (or other molecules)

A

Solvent carries amino acids up the TLC plate. The rate of movement depends on the balance between that amino acids solubility in the solvent and the affinity for the stationary phase

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16
Q

What do you often have to do to enable the amino acids to be seen on the chromatogram

A

Spray with ninhydrin (aa are colourless, turns their spots purple)
Shine UV light

17
Q

How do you find the primary structure of a protein

A

Reflux with 6M HCl and reflux for 24 hours
Carry out TLC to find the number and type of amino acids present

18
Q

How do enzymes increase the rate of reaction

A

Reacting molecules form temporary bonds (via imf) to the enzyme. This weakens the bonds in the molecules, promotes electron movement and lowers EA

19
Q

What does the stereospecificity of enzymes mean

A

Active sites are so selective of the shape of substrates that only reactions involving one enantiomer are catalysed

20
Q

What does DNA stand form=

A

Deoxyribonucleic acid

21
Q

Draw a nucleotide

A

Google

22
Q

What forms between adjacent nucleotides

A

Hydrogen bonding

23
Q

What kind of polymer does the polymerisation of DNA lead to

A

Condensation polymer chain - backbone of phosphate and sugar molecules, with bases attached

24
Q

Draw the structure of cisplatin

A

google

25
Q

What is cisplatins function and how does it do this

A

Anti cancer drug
Bonds to strands of DNA to distort shape and prevent cell replication. It bonds to the N atoms on 2 adjacent G bases. The N atoms replace the Cl- ligands in a ligand substitution reaction

26
Q

Why are Cl- ions able to be replaced by N on the base

A

N atoms on the G base have lone pairs of electrons that can co-ordinately bond to the Pt ion; N atom are better ligands than Cl-; so replace them

27
Q

What are the drawbacks of using cisplatin

A

Affects healthy cells that are replicating quickly, eg hair follicles
Thought to damage kidneys