Needs a lot of energy to
evaporate water - useful for
organisms in restoring body
temperature.
Highest specific heat capacity
of any common liquid
value: 4190 J/kg/Degree celsius
High cohesive forces
Strong cohesion makes
it flow - great as a
transport medium e.g.
xylem in plants
High surface tension
Due to high cohesive
forces. Useful for some
insects walking across
ponds (see pic),
Structure
composed of 2
hydrogen atom
and 1 oxygen
atom
Bonding
Hydrogen bonds are formed
between opposite atoms
hydrogen bonds are 1/10th the
strength of a covalent bond
(individually), Collectively,
they're quite significant.
Uses of water
Great metabolite
Good solvent
Proteins
Enzymes
2 types
Anabolic
build up substances
Catabolic
break down substances
Factors affecting
enzyme-controlled reactions
Substrate concentration
Enzyme concentration
As long as there is an excess of substrate , an
increase in enzyme leads to a proportionate
increase in rate of reaction
However, once substrate runs out...
Temperature
As temperature increases, enzyme and substrate molecules gain
more kinetic energy so they collide more frequently. this means that
more ES complexes are formed so there is a faster rate of reaction.
pH conditions
Changes alter the charges on
the amino acids making up the
active site of the enzyme
This causes hydrogen and ionic bonds to break that maintain the
tertiary structure and makes it reform in different places.
The active site has changed shape and the substrate
will not fit - the enzyme has denatured.
Rate of reaction
2 types
intracellular
work inside the cell
extracellular
work outside the cell
biological catalysts and are globular proteins
They lower the activation
energy required to start a
reaction so less energy and
time is needed for it.
models
induced fit model
more accepted model of the 2
suggests that the enzyme
active site and substrate are
NOT exactly complementary
to begin with but when a
substrate binds to an
enzyme it induces change in
enzyme structure.
The active site of the enzyme is said to be complementary as the active site
moulds itself around the substrate to make an enzyme-substrate complex
suitable analogy - hand in glove
lock and key model
taught at GCSE
Limitation - it suggests
that the enzyme
structure is rigid, which
is actually not true
This suggests that the substrate
combines with the enzyme in a
precise way - like a lock and key
Inhibitors
General
Structure
Condensation
(forming dipeptides
and polypeptides)
peptide bond
formed
This is broken in the inverse reaction
called HYDROLYSIS.
Protein structure
Primary structure
Sequence of amino acids in a
polypeptide chain
Secondary
Hydrogen bonds form
between certain
amino acids in the
chain
This makes the chain automatically coil/
fold into an alpha helix or beta pleated
sheet
Tertiary
More bonds form
between amino acids
including disulfide
bridges, hydrogen and
ionic bonds. This causes
the chain to coil further.
Quaternary
Several different polypeptide
chains join together between
bonds created to form one
final 3D structure.
Conjugated proteins
Proteins with more groups attached
Haemoglobin has haem groups
attached to it's quaternary structure
Chemical
test for
protein
Add Biuret's solution to a protein sample
few drops of NaOH and CuSO_4
Results
Negative result -
same blue colour
Positive colour -
solution turns lilac
colour
Chromatography
Carbohydrates
Monosaccharides
They are monomers that carbohydrates are made from
examples
glucose
What group are these
monosaccharides
classified as?
galactose
fructose
Glucose
Alpha glucose
Beta glucose
What is the structural
difference between these
two isomers?
Alpha:
Beta:
Disaccharides
examples
maltose
glucose + glucose
sucrose
glucose + fructose
lactose
glucose + galactose
Processes involved
condensation
forms one water
molecule and a disaccharide
hydrolysis
breaks down the disaccharide
and water to form 2
monosaccharides
Chemical Tests
Reducing sugars test
Method
Add Benedict's reagent to a sample of
sugar solution then heat in water bath for
2 minutes
Expected results
Negative
Positive
colour changes
Non reducing sugars
Method
Add dilute HCl to a sample of sugar
in test tube then boil in a water bath
for 5 mins. Remove and cool.
Neutralise acid by adding few drops
of NaOH. Dip a glass rod in then
transfer a drop onto indicator
paper. If paper BLUE add Benedict's
reagent then heat for 2 minutes.
Result
Should turn blue to orange (Benedict's)
Non-reducing sugars present
Reducing and non-reducing sugars
What are they?
Reducing sugars are sugars
that can donate electrons and
act as reducing agents.
Non-reducing sugars cannot
donate electrons (opposite of
reducing sugars)
Examples
Non-reducing
Sucrose is the
only one you need
to know about for
this course.
Reducing
All sugars except sucrose.
Structure
Bonds present
Only glycosidic
These form between
carbon-1 and
carbon-4 of each
monosaccharide
Polysaccharides
Chemical tests
Test for starch
Method
Add some iodine solution to a sample of starch. Iodine will change
from a browny-red to a specific colour that shows whether sample
has starch present.
Expected Result
Positive
Changes to a blue-black colour
Negative
Stays a browny-red colour (original colour)
Consists of TWO or more polysaccharides
Functions of polysaccharides
Starch
Mixture of 2 alpha-glucose polysaccharides
AMYLOSE and AMYLOPECTIN
Amylose
long, unbranched
chain of
alpha-glucose
compact - lots can be stored in small places
Amylopectin
Long, branched chain
of alpha-glucose
easily hydrolysed
due to many
branches
Insoluble in water - doesn't
affect water potential. Also
helical structure - makes it
compact and easy to store
Glycogen
polysaccharide of alpha-glucose
loads more side
branches than
amylopectin
compact molecule -
good for storage
Cellulose
Long, unbranched
chains of BETA glucose
chains linked by
hydrogen bonds to
form microfibrils
hydrogen bonds give high
tensile strength
Chromatography
Rf values
used to identify
monosaccharides and
amino acids in mixtures