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Organic Chemistry > Organic 13: Biochemistry > Flashcards

Organic 13: Biochemistry Flashcards

1
Q

What is a zwitterion?

A

A species that has both a positive and negative charge on different parts of the molecule

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2
Q

Why are amino acids usually solids at room temperature?

A

Due to the strong ionic attraction between opposite charges on zwitterions

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3
Q

Describe the general structure of an amino acid.

A

Central chiral carbon surrounded by hydrogen, carboxylic acid group, variable group, and amine group

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4
Q

What is the only amino acid that isn’t optically active and why?

A

Glycine
Because glycine’s variable group is hydrogen, which means there are only three different groups around the central carbon
All other amino acids are optically active but only one enantiomer is present in nature

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5
Q

How many naturally occurring amino acids are there?

A

20

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6
Q

What ion is produced at low pH on an amino acid?

A

In strongly acidic conditions, the lone pair on NH2 accepts a proton to form an NH3+ ion (is protonated)

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7
Q

What ion is produced at high pH on an amino acid?

A

In strongly alkaline conditions, the -OH group loses a hydrogen ion (is deprotonated) to form an OH- ion

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8
Q

What is an amide linkage?

A

The bond formed after condensation reaction between two amino acids

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9
Q

What is the primary structure of a protein?

A

The fixed sequence of amino acids in the polypeptide chain
It is relatively stable due to covalent bonding

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10
Q

What is the secondary structure of a protein?

A

The initial folding of a polypeptide chain into either an alpha helix or a beta-pleated sheet due to hydrogen bonding
Hydrogen bonds are much weaker than covalent bonds so the secondary structure is more easily disrupted

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11
Q

What is the tertiary structure of a protein?

A

Further folding into a three-dimensional shape held in place by hydrogen bonding, ionic bonding, and disulfide bridges

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12
Q

How is a protein hydrolysed?

A

With hydrochloric acid of concentration 6moldm-3 for about 24 hours
This hydrolyses all peptide linkages

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13
Q

How would you find the structure of proteins?

A

By refluxing the protein in 6moldm-3 hydrochloric acid to break the amide linkages (hydrolysis) resulting in a mixture of all the individual amino acids

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14
Q

Describe how you would use Thin Layer Chromatography to determine which amino acids make up a protein.

A
  1. Add a small spot containing the mixture of amino acids about 1cm up the plate
  2. Place the plate in a tank containing a suitable solvent, and put a lid on it (this allows the solvent vapours to carry the amino acids up the stationary phase)
  3. The affinity for the mobile and stationary phase depends on the intermolecular forces that act between the amino acid and each phase
  4. Mark the solvent front (how far the solvent was carried up the stationary phase)
  5. Spray the plate with ninhydrin, which reacts with amino acids to form a purple compound, OR shine ultra-violet light onto the plate to see how far the amino acids were carried
  6. Calculate the Rf value (distance moved by spot/distance moved by solvent)
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15
Q

What are enzymes?

A

Protein-based catalysts that speed up the rate of reactions
Usually globular proteins with active sites where the reaction occurs

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16
Q

What is the lock and key hypothesis?

A

The reacting molecule fits precisely into the active site and is held in the precise orientation necessary to react

17
Q

What is the reality of enzyme-substrate interactions?

A

The reacting molecule must bond to the active site temporarily by intermolecular forces (i.e. van Der Waals)
These forces allow electrons to move within the substrate to lower the activation energy for the reaction

18
Q

How is the stereospecificity of enzymes important?

A

The active site of an enzyme is selective to individual enantiomers
Because the substrate molecule must have a 3D structure that can bind precisely to the active site

19
Q

How can enzymes be denatured?

A

Changes in pH
Changes in temperature
(Too much deviation from optimum)

20
Q

What is enzyme inhibition?

A

Where a molecule with a similar shape/tertiary structure to the substrate can be used to block the active site to prevent enzyme-substrate complexes from forming

21
Q

Name one drug that works by enzyme inhibition.

A

Penicillin
Inhibits the enzymes responsible for controlling the building of cell walls in bacteria

22
Q

How is computer modelling useful in drug design?

A

Computer modelling techniques can be used to predict the shape of proteins before they have been synthesised
So can therefore predict their properties

23
Q

Describe the structure of a DNA nucleotide.

A

Phosphate
2-Deoxyribose
Organic base

24
Q

What are the four organic bases?

A

Adenine, Thymine, Cytosine, Guanine

25
Q

How can two nucleotides join together?

A

In a condensation reaction
between the -OH on a phosphate and the -OH on deoxyribose
to form a phosphodiester bond

26
Q

How many hydrogen bonds do adenine-thymine and cytosine-guanine form? (and draw the bonding)

A

Adenine and thymine = 2 bonds
Cytosine and guanine = 3 bonds

27
Q

What is the function of DNA?

A

To store genetic information needed to allow organisms to develop, survive and reproduce
Needed for formation of structural material, like flesh, and also enzymes that control biochemical reactions
Contained in every cell and must be replicated precisely during cell division

28
Q

How does DNA replication occur?

A

Hydrogen bonds between bases are individually weak so can be easily broken, leaving two free template strands
Free DNA nucleotides are attracted to the parent strand via complementary base pairing (A-T, C-G) and form hydrogen bonds
Adjacent nucleotides join in condensation reactions forming phosphodiester bonds
Resulting in two new identical double-stranded molecules of DNA

29
Q

What is cancer?

A

A group of diseases caused by the uncontrolled division of cells leading to formation of a tumour

30
Q

What is cisplatin?

A

An anti-cancer drug
Square planar
Survival rates up to 90% in testicular cancer

31
Q

How does cisplatin work?

A

Ligand substitution reaction

By bonding to strands of DNA via the nitrogen atoms, which have lone pairs
They can form dative covalent bonds with the platinum
The chloride ions are displaced by water, which are then displaced by nitrogen on guanine because nitrogen is a better ligand

32
Q

What are the side effects of cisplatin use?

A

It can also form bonds to guanine on the DNA of healthy cells
However cancer cells divide more rapidly, so the effect on cancer cells is greater
Hair follicle cells divide very rapidly, so cisplatin has a greater effect on them as well
Which is why chemotherapy patients often lose their hair

33
Q

Why would transplatin not be a good anti-cancer drug?

A

Because one chloride ion would be on the opposite side of the molecule, so would be too far apart to form bonds to guanine

Organic Chemistry (16 decks)

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