(i) amino acid chemistry:
the primary, secondary and tertiary structure of proteins; the role of intermolecular bonds in determining the secondary and tertiary structures, and hence the properties of proteins
DNA and RNA as condensation polymers formed from nucleotides, which are monomers having three components (phosphate, sugar and base): (i) the phosphate units join by condensation with deoxyribose or ribose to form the phosphate-sugar backbone in DNA and RNA (ii) the four bases present in DNA and RNA join by condensation with the deoxyribose or ribose in the phosphate-sugar backbone (iii) two strands of DNA form a double-helix structure through base pairing
Monomers of DNA and RNA are given on the Data Sheet.
the significance of hydrogen bonding in the pairing of bases in DNA and relation to the replication of genetic information; how DNA encodes for RNA which codes for an amino acid sequence in a protein
Some triplet base codes are given on the Data Sheet.
molecular recognition (the structure and action of a given pharmacologically active material) in terms of:
(i) the pharmacophore and groups that modify it (ii) its interaction with receptor sites (iii) the ways that species interact in three dimensions (size, shape, bond formation, orientation)
the shape of the rate versus substrate concentration curve for an enzyme-catalysed reaction; techniques and procedures for experiments involving enzymes
At low concentrations of substrate the order with respect to the substrate is one, at higher concentrations of substrate the order with respect to the substrate is zero.
the characteristics of enzyme catalysis, including: specificity, temperature sensitivity, pH sensitivity, competitive inhibition; explanation of these characteristics of enzyme catalysis in terms of a three-dimensional active site (part of the tertiary structure)
the acidic nature of carboxylic acids, and their reaction with metals, alkalis and carbonates
See also CD(f).
the acid–base properties of amino acids and their existence as zwitterions
the basic nature of the amino group; the reaction of amines with acids
In terms of a lone pair on the nitrogen accepting a proton to give a cation. See also CD(f).
the formulae and systematic nomenclature of members of the following homologous series: carboxylic acids, phenols, acyl chlorides, acid anhydrides, esters, aldehydes, ketones, diols, dicarboxylic acids, primary amines, diamines; naming nylon structures
The structures of nylon-6,6 nylon-6,10 and nylon-6.
the formulae for the following functional groups: primary amide, secondary amide
the hydrolysis of esters and amides by both aqueous acids and alkalis, including salt formation where appropriate
the reactions of acyl chlorides with amines and alcohols
See also CD(f).
the differences between addition and condensation polymerisation
the relationship between the structural formula of a condensation polymer and the structural formulae of its monomer(s) and vice versa
optical isomerism:
(i) diagrams to represent optical stereoisomers of molecules (ii) the use of the term chiral as applied to a molecule and identifying carbon atoms that are chiral centres in molecules (iii) enantiomers as non-superimposable mirror image molecules
the further interpretation and prediction of mass spectra:
(i) use of the high-resolution value of the M+ peak to work out a molecular formula (ii) the mass differences between peaks indicating the loss of groups of atoms
See also WM(i).
proton and carbon-13 nuclear magnetic resonance (NMR) spectra for the determination of molecular structure
Including splitting patterns up to quartets for proton NMR using the ‘n+1’ rule; further explanation of splitting not required. All carbon-13 NMR spectra that are assessed will be proton decoupled.
the combination of spectroscopic techniques (mass spectrometry, IR and NMR) to determine the structure of organic molecules