Biological molecules

TESTS
Glucose (monosaccharides) and maltose reducing sugars sucrose non-reducing
sugar
Reducing sugars tests
Benedicts reagent + heat, blue orange-red
Standard volume colour intensity compared with known concentration colour standards to
show solution concentration
Non-reducing sugars test
If not reducing sugars, hydrolyse by dilute HCl + heat + alkali
Benedicts reagent + heat, blue orange-red
Starch test
Potassium iodide solution, orange-brown blue-black
Lipids test
Pure ethanol shaken and poured into tube of water, colourless milky emulsion
Protein test
Biuret reagent, blue purple

DEFINITIONS
Monomer small molecule that can be linked to identical monomers to form a polymer
Polymer molecule made up of many monomers linked together in a long chain
Macromolecule large biological molecule e.g. polysaccharide or protein
Monosaccharide single sugar unit with formula CnH2nOn
Disaccharide substance made of two monosaccharides linked by a glycosidic bond
Polysaccharide polymer of many monosaccharides linked by glycosidic bonds in a long
chain
-glucose C1 OH group below plane
-glucose - C1 OH group above plane

GLYCOSIDIC BONDS
Formation
In condensation reaction, a disaccharide is formed as OH group and H atom combine to form
H2O and glycosidic bond between two monosaccharides
Disaccharides
Maltose -glucose
Sucrose - -glucose and -fructose
Lactose glucose and galactose
Breakage
In hydrolysis reaction, glycosidic bond in
disaccharides and polysaccharides is
broken as H2O is added
POLYSACCHARIDES
Starch is a mixture of amylose and amylopectin
Amylose
Unbranched -glucose 1,4 linkages cause chain to coil up into spiral so more compact
Amylopectin/glycogen
Shorter branched -glucose 1,4 linkages and 1,6 branch linkages (glycogen more
branched)
Branched with many ends so increased rate of carbohydrase hydrolysis

Cellulose
Straight -glucose 1,4 linkages alternate in orientation at 180 o
Makes up cell walls in plants due to high mechanical strength
Many hydrogen bonds within cellulose molecule
Cellulose molecules lie side by side to form parallel chains as the hydrogen bonds
between cellulose molecules form microfibrils, which are held together by more
hydrogen bonds to form fibres

TRIGLYCERIDE
Structure
Glycerol alcohol bonded to three fatty acids by ester bonds - glycerol contains three OH
groups which each bond to COOH group on acid to form ester bond and H 2O in condensation
reaction
Unsaturated lipids - C=C double bonds in fatty acid reduce melting point
Energy storage compound
Water insoluble non-polar and hydrophobic fatty acid tails
Energy per gram higher than polysaccharides so more energy stored in less mass

Other functions
Adipose tissue beneath mammal skin for heat insulation and aquatic mammals for
buoyancy
Metabolic source of water can be oxidised during respiration to form CO 2 and H2O

PHOSPHOLIPID
Structure
Hydrophilic head as fatty acid tail replaced with polar phosphate group and hydrophobic tail
as fatty acid tails are non-polar
Function
Phospholipids form a bilayer in water with hydrophilic heads facing outwards into water and
hydrophobic tails facing inwards to avoid water contact, this forms cell membrane structure

AMINO ACID
Structure
Carbon atom bonded to NH2 and COOH group, H atom, and a
differing R side chain
Formation
In condensation reaction, OH group and H atom combine to form peptide bond between
carbon and nitrogen of two amino acids and water molecule
Breakage
In hydrolysis reaction, peptide bond is broken down as H 2O is added

PROTEIN STRUCTURE
The tertiary and quaternary structure of a protein, and therefore its function, is determined by
its primary structure
Primary structure - sequence of amino acids in polypeptide chain
Secondary structure - first level of folding of polypeptide chain - hydrogen bonds cause
polypeptide to coil into -pleated sheet or -helix shape
Tertiary structure - second level of folding of polypeptide chain
Hydrogen bonds by polar groups (-NH, -CO and -OH) can be broken by high
temperatures and pH changes
Disulfide bonds by sulfur containing molecules are covalent and can be broken by
reducing agents
Ionic bonds by ionised amine (NH3+) and carboxylic acid (COO-) groups can be broken
by pH changes
Weak hydrophobic interactions by non-polar R groups stay together while repelled by
water environment

Quaternary structure - association of two or more polypeptide chains

Haemoglobin - primary structure sequence of amino acids / secondary structure -
helices / tertiary structure folding of each polypeptide / quaternary structure four
polypeptides

GLOBULAR PROTEINS
Spherical proteins that have a tertiary structure and are water soluble because of hydrophilic
groups on outside
Haemoglobin
Globular protein with four polypeptide chains, two -chains and two -chains, that transports
oxygen
Soluble
Globular protein structure is water soluble as hydrophilic R groups form hydrogen bonds
with water on outside while hydrophobic R groups avoid water contact on inside
Combines with oxygen
Polypeptide chain has haem group with an iron ion (Fe 2+) which combines with oxygen
(O2)
Haemoglobin can combine with four oxygen molecules which is eight oxygen atoms
Oxygen affinity
Haem group bonded to oxygen molecule changes haemoglobin shape and increases its
affinity for oxygen
Picks up oxygen in high concentration, and releases oxygen in low concentration

FIBROUS PROTEIN
Long, thin water insoluble molecules which form fibres
Collagen
Fibrous protein with three helical polypeptide chains wound and held together by hydrogen
bonds, to form a three stranded triple helix, that provides support and elasticity
Unlike haemoglobin, collagen protein has a triple helix structure, no prosthetic group, no
complex folding, is not globular and its polypeptides are not identical
Insoluble
Too long and large to dissolve in water
High tensile strength
Three stranded triple helix held by hydrogen bonds withstands high pulling force and
creates elasticity
Compact
Every third amino acid in polypeptide is glycine, small size due to single hydrogen R
group allows polypeptides to pack tightly

Fibres
Hydrogen bonds between collagen R groups form microfibrils which form strong
collagen fibres

WATER
Hydrogen bonding
Water molecule has slightly negative charge (-) on oxygen atom and slightly positive charge
(+) on hydrogen atoms
Hydrogen bond formed from attraction between + and - parts of neighbouring water
molecules

Solvent
Slightly charged water molecules attracted to ions and polar molecules, surrounding,
separating and dissolving them
Solvent property of water allows it to transport substances in organisms and be a medium for
metabolic reactions
High latent heat of vapourisation
Large amount of energy required to break hydrogen bonds before gaining kinetic energy and
evaporating
Absorbs heat from surroundings when evaporating, used in sweat and transpiration for cooling
High specific heat capacity
Large amount of energy required to break hydrogen bonds before gaining kinetic energy to
increase temperature
Large bodies of water change temperature more slowly, providing stable habitats for aquatic
organisms
Metabolic reactions occur are less affected by temperature changes
Organism bodies change temperatures more slowly