2.1.1: cell structure
- the use of microscopy to observe and
investigate different types of cell and cell
structure in a range of eukaryotic organisms
(including light, TEM, SEM, and LSC
microscopes)
- the preparation and examination of
microscope slides for use in light microscopy
(including the use of eyepiece graticule and
stage micrometre)
- the use of staining in light microscopy
(including the use of differential staining)
- the representation of cell structure as seen
under the light microscope using drawings
and annotated diagrams of whole cells or
cells in sections of tissue
- the use and manipulation of the
magnification formula
- the difference between magnification and
resolution (including differences in
microscopes)
- the ultrastructure of eukaryotic cells and the
functions of different cellular components
(including nucleus, nucleolus, nuclear
envelope, rough and smooth endoplasmic
reticulum, Golgi apparatus, ribosomes,
mitochondria, lysosomes, chloroplasts,
plasma membrane, centrioles, cell wall,
flagella, and cilia)
- photomicrographs of cellular components in a
range of eukaryotic cells (including
interpretation of TEM and SEM images)
, - the interrelationship between organelles
involved in the production and secretion of
proteins
- the importance of the cytoskeleton (including
mechanical strength to cells, aiding transport
within cells, and enabling cell movement)
- the similarities and differences in the
structure and ultrastructure of prokaryotic
and eukaryotic cells (PAG 1)
2.1.2: biological molecules
- how hydrogen bonding occurs between water
molecules, and relate this, and other
properties of water, to the roles of water for
living organisms (including range of roles
including solvent, transport medium, coolant,
and as a habitat, and roles illustrated using
examples of prokaryotes and eukaryotes)
- the concept of monomers and polymers and
the importance of condensation and
hydrolysis reactions in a range of biological
molecules
- the chemical elements that make up
biological molecules: C,H,O for
carbohydrates, C,H,O for lipids, C,H,O,N,S for
proteins, and C,H,O,N,P for nucleic acids
- the ring structure and properties of glucose
as an example of a hexose monosaccharide
and the structure of ribose as an example of
, a pentose monosaccharide (including the
structural difference between an α- and a β-
glucose, and the difference between a
hexose and a pentose monosaccharide)
- the synthesis and breakdown of a
disaccharide and polysaccharide by the
formation and breakage of glycosidic bonds
(including the disaccharides: sucrose,
lactose, and maltose)
- the structure of starch: amylose and
amylopectin, glycogen, and cellulose
molecules
- how the structures and properties of glucose,
starch, glycogen, and cellulose molecules
relate to their functions in living organisms
- the structure of a triglyceride and a
phospholipid as examples of macromolecules
(including an outline of saturated and
unsaturated fatty acids)
- the synthesis and breakdown of triglycerides
by the formation/esterification and breakage
of ester bonds between fatty acids, and
glycerol
- how the properties of triglyceride,
phospholipids, and cholesterol molecules
relate to their functions in living organisms
(including hydrophobic and hydrophilic
regions and energy content, and illustrated
using examples of prokaryotes and
eukaryotes)
- the general structure of an amino acid
, - the synthesis and breakdown of dipeptides
and polypeptides, by the formation and
breakage of peptide bonds
- the levels of protein structure (including
primary, secondary, tertiary, and quaternary
structure, and hydrogen bonding,
hydrophobic and hydrophilic interactions,
disulphide bonds, and ionic bonds)
- the structure and function of globular
proteins including a conjugated protein
(including haemoglobin as an example of a
conjugated protein-a globular protein with a
prosthetic group, a named enzyme, and
insulin) (PAG 10)
- the properties and functions of fibrous
proteins (including collagen, keratin, and
elastin)
- the key inorganic ions that are in involved in
biological processes- cations: calcium ions
Ca2+, sodium ions Na+, potassium ions K+,
hydrogen ions H+, and ammonium ions NH4+,
and anions: nitrate NO3-, hydrogencarbonate
HCO3-, chloride Cl-, phosphate PO43-, and
hydroxide OH-
- how to carry out and interpret the results of
the following chemical tests: biuret tests for
proteins, Benedict’s test for reducing and
non-reducing sugars, reagent test strips for
reducing sugars, iodine test for starch, and
emulsion test for lipids (PAG 9)
- quantitative methods to determine the
concentration of a chemical substance in a
- the use of microscopy to observe and
investigate different types of cell and cell
structure in a range of eukaryotic organisms
(including light, TEM, SEM, and LSC
microscopes)
- the preparation and examination of
microscope slides for use in light microscopy
(including the use of eyepiece graticule and
stage micrometre)
- the use of staining in light microscopy
(including the use of differential staining)
- the representation of cell structure as seen
under the light microscope using drawings
and annotated diagrams of whole cells or
cells in sections of tissue
- the use and manipulation of the
magnification formula
- the difference between magnification and
resolution (including differences in
microscopes)
- the ultrastructure of eukaryotic cells and the
functions of different cellular components
(including nucleus, nucleolus, nuclear
envelope, rough and smooth endoplasmic
reticulum, Golgi apparatus, ribosomes,
mitochondria, lysosomes, chloroplasts,
plasma membrane, centrioles, cell wall,
flagella, and cilia)
- photomicrographs of cellular components in a
range of eukaryotic cells (including
interpretation of TEM and SEM images)
, - the interrelationship between organelles
involved in the production and secretion of
proteins
- the importance of the cytoskeleton (including
mechanical strength to cells, aiding transport
within cells, and enabling cell movement)
- the similarities and differences in the
structure and ultrastructure of prokaryotic
and eukaryotic cells (PAG 1)
2.1.2: biological molecules
- how hydrogen bonding occurs between water
molecules, and relate this, and other
properties of water, to the roles of water for
living organisms (including range of roles
including solvent, transport medium, coolant,
and as a habitat, and roles illustrated using
examples of prokaryotes and eukaryotes)
- the concept of monomers and polymers and
the importance of condensation and
hydrolysis reactions in a range of biological
molecules
- the chemical elements that make up
biological molecules: C,H,O for
carbohydrates, C,H,O for lipids, C,H,O,N,S for
proteins, and C,H,O,N,P for nucleic acids
- the ring structure and properties of glucose
as an example of a hexose monosaccharide
and the structure of ribose as an example of
, a pentose monosaccharide (including the
structural difference between an α- and a β-
glucose, and the difference between a
hexose and a pentose monosaccharide)
- the synthesis and breakdown of a
disaccharide and polysaccharide by the
formation and breakage of glycosidic bonds
(including the disaccharides: sucrose,
lactose, and maltose)
- the structure of starch: amylose and
amylopectin, glycogen, and cellulose
molecules
- how the structures and properties of glucose,
starch, glycogen, and cellulose molecules
relate to their functions in living organisms
- the structure of a triglyceride and a
phospholipid as examples of macromolecules
(including an outline of saturated and
unsaturated fatty acids)
- the synthesis and breakdown of triglycerides
by the formation/esterification and breakage
of ester bonds between fatty acids, and
glycerol
- how the properties of triglyceride,
phospholipids, and cholesterol molecules
relate to their functions in living organisms
(including hydrophobic and hydrophilic
regions and energy content, and illustrated
using examples of prokaryotes and
eukaryotes)
- the general structure of an amino acid
, - the synthesis and breakdown of dipeptides
and polypeptides, by the formation and
breakage of peptide bonds
- the levels of protein structure (including
primary, secondary, tertiary, and quaternary
structure, and hydrogen bonding,
hydrophobic and hydrophilic interactions,
disulphide bonds, and ionic bonds)
- the structure and function of globular
proteins including a conjugated protein
(including haemoglobin as an example of a
conjugated protein-a globular protein with a
prosthetic group, a named enzyme, and
insulin) (PAG 10)
- the properties and functions of fibrous
proteins (including collagen, keratin, and
elastin)
- the key inorganic ions that are in involved in
biological processes- cations: calcium ions
Ca2+, sodium ions Na+, potassium ions K+,
hydrogen ions H+, and ammonium ions NH4+,
and anions: nitrate NO3-, hydrogencarbonate
HCO3-, chloride Cl-, phosphate PO43-, and
hydroxide OH-
- how to carry out and interpret the results of
the following chemical tests: biuret tests for
proteins, Benedict’s test for reducing and
non-reducing sugars, reagent test strips for
reducing sugars, iodine test for starch, and
emulsion test for lipids (PAG 9)
- quantitative methods to determine the
concentration of a chemical substance in a
