OCR A-Level Chemistry B H433
Development of Practical Skills in Chemistry
Elements of Life
Developing Fuels
Elements From the Sea
The Ozone Story
What's in a Medicine?
The Chemical Industry
Polymers and Life
Oceans
Developing Metals
Colour by Design
Chemical Literacy
Mathematical Skills in Chemistry
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.
- Amino acids, the peptide link and hydrolysing a proteinRecall questions on the general formula of an amino acid, which groups form the peptide link and what is lost, and the products of acid and alkaline hydrolysis.Open →
- Chromatography of amino acids and Rf valuesRecall questions on the baseline and solvent front, why a locating agent is needed, ninhydrin, and calculating and using an Rf value.Open →
- Protein structureRecall questions on primary, secondary and tertiary structure, the interactions between side chains, disulfide bridges, and fibrous against globular proteins.Open →
- DNA and RNA structureRecall questions on the sugars, the nucleotide monomer, the phosphate backbone, and how RNA differs from DNA in structure and stability.Open →
- Base pairing and the genetic codeRecall questions on which bases pair and by how many hydrogen bonds, why replication is semi-conservative, and reading an amino acid sequence from codons.Open →
- Molecular recognitionRecall questions on why shape and functional groups decide activity, why drug-receptor bonds must be weak, and why only some related compounds work.Open →
- Enzyme kineticsRecall questions on the shape of the rate-concentration curve, why it is first order then zero order, and why it levels off.Open →
- Characteristics of enzyme catalysisRecall questions on specificity, the effect of temperature and pH, the optimum, and why denaturation is not reversed on cooling.Open →
- Acidity of carboxylic acidsRecall questions on why a carboxylic acid is acidic, its reactions with metals, carbonates and alkalis, and why a phenol gives no effervescence.Open →
- Amino acids as zwitterionsRecall questions on why a zwitterion forms, the isoelectric point, and why amino acids melt high and dissolve well in water.Open →
- Basicity of aminesRecall questions on why the nitrogen lone pair makes an amine basic, the salt formed with an acid, and the smell and solubility of short-chain amines.Open →
- Naming acids, acyl chlorides, anhydrides, esters, aldehydes and ketonesRecall questions on the suffix for each series, writing a structural formula from a name, and naming a compound from its structure.Open →
- Diols, dicarboxylic acids, amines, amides and the nylonsRecall questions on naming diols and dicarboxylic acids, the primary and secondary amide groups, and the monomers behind nylon-6,6 and nylon-6.Open →
- Hydrolysis of esters and amidesRecall questions on acid and alkaline hydrolysis of an ester and an amide, why the alkaline route goes to completion, and recovering the free acid.Open →
- Reactions of acyl chloridesRecall questions on why an acyl chloride is so reactive, and its reactions with water, alcohols and amines and what is observed.Open →
- Condensation polymerisationRecall questions on what is eliminated, which monomer pairs give a polyester and which a polyamide, and deducing a repeat unit or the monomers.Open →
- Optical isomerismRecall questions on what a chiral centre is, identifying one in a structure, why the isomers are drawn in three dimensions, and racemic mixtures.Open →
- Further interpretation of mass spectraRecall questions on accurate mass and why it separates compounds of the same nominal mass, and identifying fragments lost from a molecular ion.Open →
- Chemical shift and equivalent protons in proton NMRRecall questions on the TMS reference, what chemical shift depends on, equivalent protons, and the shift ranges for the common environments.Open →
- The n + 1 rule, integration and carbon-13 NMRRecall questions on the splitting patterns and what they show, what the integration trace gives, and how a carbon-13 spectrum is read.Open →
- Combined spectroscopic structure determinationRecall questions on combining infrared, mass spectrometry and NMR, and on working a structure out from a set of spectra.Open →
What you need to know
Answer each one before you reveal it.
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?
Why is a chromatogram baseline drawn in pencil, why is a locating agent needed for amino acids, and which locating agent is used?
Why can an Rf value never be greater than 1?
Which part of a residue gives tertiary interactions, where do disulfide bridges form, and how do fibrous and globular proteins differ?
Does denaturing a protein change its primary structure? Explain.
Which sugar is in DNA and which in RNA, how do the two sugars differ, and how is a base attached to the backbone?
Which DNA base is replaced in RNA, which bases are purines, and which part of a nucleotide varies along a strand?
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?
Why is it an advantage that the forces between the two strands are relatively weak?
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?
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)?
Why does the primary structure alone determine a protein's function?
Why can a change of one base sometimes have no effect at all on the protein?
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?
Why can one optical isomer of a drug be active while its mirror image is not?
How does knowing the shape of a receptor site help in designing a medicine?
How does the shape of the curve show first order at low substrate and zero order at high, and why?
What is the unit of a first-order rate constant, what does doubling the enzyme do, and why does the curve level off?
Why are initial rates measured, why is temperature control critical, and how is a coloured product followed?
Why is a very small amount of enzyme normally enough?
Why does the rate rise towards the optimum temperature, fall steeply above it, and not recover on cooling?
What would you observe about the maximum rate of a reaction in the presence of a competitive inhibitor?
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?
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?
Why does magnesium react less vigorously with ethanoic acid than with hydrochloric acid of the same concentration?
Why does an amino acid exist as a zwitterion, and why does that give high melting points and good water solubility?
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?
What is the primary amine functional group, why is it basic, and what forms when it accepts a proton?
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?
Why is an amide much less basic than an amine?
Which suffixes identify a carboxylic acid and an acyl chloride, and how is an ester named?
What suffix is used for an aldehyde, and where must its functional group lie?
Why does hexanedioic acid keep the number six in its name even though only four CH₂ groups appear?
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?
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?
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?
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?
What is the equation for ethanoyl chloride with methylamine, why is excess amine used, and which part attacks?
Name the ester and the other product formed when propanoyl chloride reacts with methanol.
How can you tell from the repeat unit that a polymer is a polyamide rather than a polyester?
Why do many condensation polymers slowly weaken in a damp environment?
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?
Why does a reaction catalysed by an enzyme usually give only one enantiomer?
Why is optical isomerism a form of stereoisomerism rather than structural isomerism?
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?
Why must an accurate mass be quoted to four decimal places, and what is lost to give peaks at 138 and 120 from 180?
Why can a mass difference alone sometimes not identify the group lost with certainty?
How can a series of mass differences help build up a structure?
Which compound is the NMR reference, how many peaks does ethanol give, and what does a triplet indicate?
Predict the splitting patterns of the two proton signals of bromoethane, CH₃CH₂Br.
Why does the CH₃ signal of propanone appear as a single peak?
Why is it worth starting from the high-resolution molecular ion rather than the infrared spectrum?
Why can mass spectrometry not usually decide between two isomers on its own?
Between which residues do disulfide bridges form?
Which two functional groups give an amino acid its acid–base behaviour?
What suffix identifies an acyl chloride?
Compare the mass of the repeat unit with the mass of the monomers in each type of polymerisation.
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
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
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
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
Name the link that joins two amino acids together.
Model answer
The peptide link, –CO–NH–, which is an amide link.
- 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
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.
What is inside Levo
Six ways to work the same material.
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.
Every question in Polymers and Life, on a schedule.
Attempt a question from memory, write the correct version, then attempt it again. Levo records the jump between your first attempt and your last, and brings each question back on the day you are due to forget it.
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