4 Biochemistry Proteins & chemical tests
Recall the general structure of an amino acid.
Describe the synthesis and breakdown of dipeptides and polypeptides, by the formation and breakage of peptide bonds.
Describe the levels of protein structure; primary, secondary, tertiary and quaternary, include hydrogen bonding, hydrophobic/hydrophilic interactions, disulfide bonds and ionic bonds.
Describe the structure and function of globular proteins including a conjugated protein (haemoglobin) a named enzyme and insulin.
Describe the properties and functions of fibrous proteins; collagen, keratin and elastin.
Recall the key inorganic ions that are involved in biological processes: cations: calcium ions (Ca2+), sodium ions (Na+), potassium ions (K+), hydrogen ions (H+) and ammonium ions (NH4+)
Recall the key inorganic ions that are involved in biological processes: anions: nitrate (NO3–), hydrogen carbonate (HCO3–), chloride (Cl –), phosphate (PO43–), hydroxide, (OH–).
Describe how to carry out the: biuret test for proteins, Benedict’s test for reducing/non-reducing sugars, reagent test strips for reducing sugars, iodine test for starch and emulsion test for lipids.
Describe the quantitative methods to determine the concentration of a chemical substance in a by colorimetry and the use of biosensors.
Describe the principles and uses of paper and thin layer chromatography to separate biological molecules/compounds, include calculation of retention (Rf) values.