(i) the basic structure of an amino acid and the formation of peptide bonds
(ii) the use of chromatography in the separation and identification of amino acids
*To include calculation of retention (Rf) values.
Practical work to be carried out in accordance with current CLEAPSS® guidelines with regards to the risks associated with the use of ninhydrin. PAG6*
the molecular structure of globular proteins as illustrated by the structure of enzymes and haemoglobin
To include primary, secondary and tertiary structure in relation to enzymes, and quaternary structure and prosthetic groups in relation to haemoglobin.
how the structure of globular proteins enable enzyme molecules to catalyse specific metabolic reactions
To include the role of tertiary structure in the specificity of the active site, the formation of enzyme substrate complexes and the lowering of the activation energy.
(i) the factors affecting the rate of enzyme-catalysed reactions
PAG4
(ii) practical investigations into the factors affecting the rate of enzyme-catalysed reactions
(i) the role of proteins in blood clotting, and blood clotting as an enzyme-controlled process
To include the role of platelets, damaged tissue, thromboplastin, calcium ions, prothrombin, thrombin, fibrinogen and fibrin.
(ii) the first-aid procedure to assist the blood clotting process and prevent excessive blood loss
the use of enzymes and inhibitors in medical diagnosis and treatment
To include diagnostic enzymes (e.g. blood amylase and LDH) and enzymes and inhibitors used in medical treatment (e.g. streptokinase, aspirin and warfarin).
the donation of blood, and the types and uses of stored blood products
To include blood groups and a consideration of the other issues affecting blood donation AND the collection and use of whole blood, leuco-depleted blood, packed red cells, platelets, clotting factors and plasma.