Polymers And Life Flashcards

1
Q

Give the products of the following reactions:
• Acid + Base/Alkali
• Acid + Metal
• Acid + Carbonate

A

• Salt + Water
• Salt + Hydrogen
• Salt + Water + Carbon Dioxide

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2
Q

Give the structure of Ethanoyl Chloride

A

CH3COCl (Must have C=O and C-Cl)

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3
Q

What conditions and reagents are required for esterification?

A

• Alcohol and Carboxylic Acid OR Alcohol and Acid Anhydride OR Alcohol and Acyl Chloride OR
Phenol and Acid Anhydride OR
Phenol and Acyl Chloride
• Few drops of conc. acid catalyst
• Boil under reflux

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4
Q

What defines whether an amine is Primary, Secondary, or Tertiary?

A

The number of Carbons the Nitrogen is bonded to

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5
Q

Give the structure of an amide bond AND state how it can form

A

• RCONHR’ (C=O, C-N, N-H)
• Can occur via a condensation reaction with a Carboxylic Acid, Acid Anhydride, Acyl Chloride

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6
Q

Give two properties of amines that affect how they react

A

• Base
• Nucleophile
• Ligand

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7
Q

Draw the repeat unit of Nylon 6,10

A

-(-NH(CH2)6NHCO(CH2)8CO-)-n
(Amide bonds drawn correctly)

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8
Q

At room temperature, amino acids are crystalline solids with high MP. Explain why

A

• This is because amino acids exist as zwitterions, so form very strong ionic bonds between molecules
• Meaning a lot of energy is required to break these bonds

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9
Q

Give the reagents and conditions for hydrolysis reactions (of proteins/esters/amides) in the lab

A

• MODERATELY conc. AQUEOUS acid/alkali solution (Ideally HCl or NaOH)
• Boil under reflux

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10
Q

Give the differences between a chromatography experiment for amino acids and one for aspirin

A

• Aspirin can work with either paper chromatography or TLC, whereas amino acids primarily use paper chromatography
• Ninhydrin solution is used instead of Iodine/UV to locate the amino acids spots. It turns purple in the presence of amino acids

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11
Q

State and explain the requirement for a molecule to exhibit enantiomerism

A

• Must contain a chiral/asymmetric carbon that is bonded to 4 different groups/atoms
• So forms two possible molecules that are mirror images of one another and are non-superimposable onto each other

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12
Q

Define the tertiary structure of a protein

A

It is the OVERALL 3D SHAPE that arises due to IDID, hydrogen, ionic, and disulfide (covalent) bonding caused by the folding of the tertiary structure

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13
Q

Describe the secondary structure of a protein

A

Section of the protein chain folded into an alpha helix or beta pleated sheet due to hydrogen bonds between amino acids

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14
Q

What is the pharmacophore of a molecule?

A

The PART OF THE MOLECULE that is responsible for it’s medicinal/biological properties

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15
Q

Describe how an enzyme works

A

• Active site of enzyme is determined by specific tertiary structure and is complementary to a specific substrate
• Substrate fits into/binds with active site
• Bonds within the substrate weaken
• Substrate reacts/breaks apart
• Products leave the active site

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16
Q

Describe how a competitive inhibitor works

A

• Inhibitor has a similar shape to substrate/is complementary to the shape of the active site
• It blocks the active site, taking up space and preventing substrate from binding
• So no active sites are available for reaction, so no reaction

17
Q

Give 5 ways that an enzyme can bond to a substrate molecule

A

• Hydrogen bonding
• Ionic bonding
• Ion-dipole bonding
• Dative covalent bonding
• IDID bonding

18
Q

Describe the structure of DNA

A

• DNA is a condensation polymer formed from nucleotide monomers. • Each nucleotide consists of a sugar, a phosphate, and a base
• Two strands of DNA arranged antiparralel with hydrogen bonds between complementary base pairs to create one DNA molecule

19
Q

Which functional group on a molecule of tRNA carries the amino acid? What bond does it form with the amino acid?

A

• OH/Alcohol group
• Forms an ester bond

20
Q

What reagent can be used to turn propan-2-ol into 2-aminopropane?

A

NH3/Ammonia

21
Q

If a reactant is second order, then ___ molecules of this reactant must react in the RDS

A

Two