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Polymers and Life

  • 21 subtopics
  • 59 things to know
  • Components 01, 02 and 03

What Polymers and Life covers

The storyline that carries the nitrogen-containing groups and the biological polymers: amino acids and proteins, DNA and RNA, enzymes as catalysts, acids, amines and amides, condensation polymerisation, optical isomerism, and NMR.

Where it is assessed

Components 01, 02 and 03

Storyline content, drawn on by all three written papers.

Check the OCR specification ↗

The 21 subtopics

Each one has its own page.

What you need to know

Answer each one before you reveal it.

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Numbers

What is the general formula of an amino acid, which carbon carries the amino group, and what link joins two of them?

Key term

Which groups react to form a peptide link and what is eliminated, how many peptide links are in a polypeptide of eight amino acid residues, and what does alkaline hydrolysis of a peptide give?

Key term

Why is a chromatogram baseline drawn in pencil, why is a locating agent needed for amino acids, and which locating agent is used?

Key term

Why can an Rf value never be greater than 1?

Key term

Which part of a residue gives tertiary interactions, where do disulfide bridges form, and how do fibrous and globular proteins differ?

Process

Does denaturing a protein change its primary structure? Explain.

Process

Which sugar is in DNA and which in RNA, how do the two sugars differ, and how is a base attached to the backbone?

Key term

Which DNA base is replaced in RNA, which bases are purines, and which part of a nucleotide varies along a strand?

Process

Why is the outside of the double helix water soluble, how does the structure of RNA differ from DNA overall, and why is DNA more stable than RNA?

Evaluation

Why is it an advantage that the forces between the two strands are relatively weak?

Process

Why is a cytosine and guanine rich region harder to separate, what does complementary base pairing mean, and how does base pairing allow exact copying?

Process

Why does replication leave one old strand in each molecule, and what amino acid sequences come from codons GGU GCC CUG (glycine, alanine, leucine) and from coding DNA GAT CAA GTC (GAU aspartic acid, CAA glutamine, GUC valine)?

Process

Why does the primary structure alone determine a protein's function?

Key term

Why can a change of one base sometimes have no effect at all on the protein?

Numbers

Why can two different drugs share an effect, why must the bonds holding a drug to a receptor be weak, and why do only some of a series of related compounds show activity?

Key term

Why can one optical isomer of a drug be active while its mirror image is not?

Process

How does knowing the shape of a receptor site help in designing a medicine?

Numbers

How does the shape of the curve show first order at low substrate and zero order at high, and why?

Numbers

What is the unit of a first-order rate constant, what does doubling the enzyme do, and why does the curve level off?

Numbers

Why are initial rates measured, why is temperature control critical, and how is a coloured product followed?

Key term

Why is a very small amount of enzyme normally enough?

Numbers

Why does the rate rise towards the optimum temperature, fall steeply above it, and not recover on cooling?

Numbers

What would you observe about the maximum rate of a reaction in the presence of a competitive inhibitor?

Numbers

What is the equation for ethanoic acid with sodium carbonate, why is the carbonate reaction a useful test for a carboxylic acid, and why does a phenol give no effervescence?

Numbers

What are the products when a carboxylic acid reacts with an alkali and with a reactive metal, and what is the equation for propanoic acid with sodium hydroxide?

Numbers

Why does magnesium react less vigorously with ethanoic acid than with hydrochloric acid of the same concentration?

Key term

Why does an amino acid exist as a zwitterion, and why does that give high melting points and good water solubility?

Numbers

What are the equations for glycine with hydrochloric acid and with sodium hydroxide, and would an amino acid with a –COOH in its side chain have an isoelectric point above or below 7?

Numbers

What is the primary amine functional group, why is it basic, and what forms when it accepts a proton?

Key term

What is seen when a volatile amine meets hydrogen chloride fumes, why do short-chain amines dissolve well in water, and why is the amino group of an amino acid protonated at low pH?

Key term

Why is an amide much less basic than an amine?

Key term

Which suffixes identify a carboxylic acid and an acyl chloride, and how is an ester named?

Key term

What suffix is used for an aldehyde, and where must its functional group lie?

Key term

Why does hexanedioic acid keep the number six in its name even though only four CH₂ groups appear?

Numbers

What is the equation for the acid hydrolysis of ethyl ethanoate, why is it an equilibrium, and what is the equation for methyl propanoate with sodium hydroxide?

Numbers

Why does alkaline hydrolysis of an ester go to completion, how is the free carboxylic acid recovered, and what is the equation for ethanamide with hydrochloric acid?

Numbers

What are the products when ethanamide is hydrolysed by sodium hydroxide, when a secondary amide is hydrolysed by aqueous alkali, and when nylon-6,6 is hydrolysed by hot concentrated acid?

Numbers

Why is an acyl chloride more reactive than the carboxylic acid, and what is the equation for, and what is seen when, ethanoyl chloride meets ethanol?

Numbers

What is the equation for ethanoyl chloride with methylamine, why is excess amine used, and which part attacks?

Key term

Name the ester and the other product formed when propanoyl chloride reacts with methanol.

Key term

How can you tell from the repeat unit that a polymer is a polyamide rather than a polyester?

Key term

Why do many condensation polymers slowly weaken in a damp environment?

Process

How do you decide whether a carbon is a chiral centre, why must enantiomers be drawn three-dimensionally, and why does a laboratory synthesis give a racemic mixture?

Key term

Why does a reaction catalysed by an enzyme usually give only one enantiomer?

Key term

Why is optical isomerism a form of stereoisomerism rather than structural isomerism?

Numbers

Why do compounds of the same nominal mass differ in accurate mass, which atom is the standard, and how does an M⁺ at m/z 180.0420 fit C₉H₈O₄?

Numbers

Why must an accurate mass be quoted to four decimal places, and what is lost to give peaks at 138 and 120 from 180?

Key term

Why can a mass difference alone sometimes not identify the group lost with certainty?

Key term

How can a series of mass differences help build up a structure?

Numbers

Which compound is the NMR reference, how many peaks does ethanol give, and what does a triplet indicate?

Key term

Predict the splitting patterns of the two proton signals of bromoethane, CH₃CH₂Br.

Key term

Why does the CH₃ signal of propanone appear as a single peak?

Numbers

Why is it worth starting from the high-resolution molecular ion rather than the infrared spectrum?

Numbers

Why can mass spectrometry not usually decide between two isomers on its own?

Key term

Between which residues do disulfide bridges form?

Key term

Which two functional groups give an amino acid its acid–base behaviour?

Key term

What suffix identifies an acyl chloride?

Key term

Compare the mass of the repeat unit with the mass of the monomers in each type of polymerisation.

Key term

Which compound is used as the reference standard in NMR, and what shift is it given?

Take Polymers and Life further

The same content, four other ways.

Commonly confused

Pairs that lose marks when they are blurred together.

  • Addition polymerisation vs Condensation polymerisation

    Addition polymerisation: monomers joining across a double bond with no other product formed. Condensation polymerisation: monomers joining with a small molecule such as water eliminated each time.

  • Peptide link vs Ester link

    Peptide link: the amide linkage joining two amino acid residues. Ester link: the linkage formed between a carboxylic acid group and an alcohol group.

  • Zwitterion vs Isoelectric point

    Zwitterion: a species carrying both a positive and a negative charge but neutral overall. Isoelectric point: the pH at which an amino acid carries no overall charge.

Questions from this topic

Each one with the model answer underneath.

  1. 1

    Which four groups are bonded to the central carbon atom of an amino acid?

    Model answer

    An amino group NH₂, a carboxyl group COOH, a hydrogen atom and a side chain R.

  2. 2

    Give the general formula of an amino acid.

    Model answer

    The general formula is RCH(NH₂)COOH, where R is the side chain that differs from one amino acid to the next.

  3. 3

    Which carbon atom in an amino acid carries the amino group?

    Model answer

    The carbon atom immediately next to the carboxyl group, so the amino group is always on carbon 2.

  4. 4

    Name the link that joins two amino acids together.

    Model answer

    The peptide link, –CO–NH–, which is an amide link.

  5. 5

    Which two functional groups react when a peptide link forms, and what is eliminated?

    Model answer

    The COOH of one amino acid reacts with the NH₂ of another, and a molecule of water is eliminated.

  6. 6

    Why are proteins classified as condensation polymers rather than addition polymers?

    Model answer

    Their monomers join with the loss of a small molecule, water, at every link, so the repeat unit is lighter than the monomer it came from.

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Polymers and Life revision questions

What does Polymers and Life cover in OCR A-Level Chemistry B?
21 subtopics: amino acids, the peptide link and hydrolysing a protein, chromatography of amino acids and rf values, protein structure, dna and rna structure, base pairing and the genetic code, molecular recognition, enzyme kinetics, characteristics of enzyme catalysis, acidity of carboxylic acids, amino acids as zwitterions, basicity of amines, naming acids, acyl chlorides, anhydrides, esters, aldehydes and ketones, diols, dicarboxylic acids, amines, amides and the nylons, hydrolysis of esters and amides, reactions of acyl chlorides, condensation polymerisation, optical isomerism, further interpretation of mass spectra, chemical shift and equivalent protons in proton nmr, the n + 1 rule, integration and carbon-13 nmr and combined spectroscopic structure determination. Each one has its own page with questions and model answers.
How is Polymers and Life organised?
By the OCR H433 specification, subtopic by subtopic, so it matches the order you are taught it in.

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