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Monomers
are small repeating units which
polymers
are made from. Examples include monosaccharides and amino acids.
Polymers
are large molecule made from
multiple
monomers
Condensation
: Joins two molecules together releasing water
Hydrolysis
: Breaks bond between molecules using water
3 types of monosaccharides:
Glucose
Galactose
Fructose
3
types of disaccharides:
Maltose (glucose +
glucose
)
Sucrose (
glucose
+
fructose
)
Lactose (
glucose
+
galactose
)
The
3 polysaccharides:
Glycogen
Starch
Cellulose
Glycogen
:
alpha
glucose
used as an
energy storage
in animals
coiled
,
branched
and compact
insoluble
so doesn't affect
water potential
contains 1,4 and 1,6
glycosidic
bonds
Starch
:
alpha
glucose
1,
4
and 1,
6
glycosidic bonds
insoluble
so doesn't affect
water potential
helical
and
compact
large
molecule so cannot
leave
the cell
amylose =>
unbranched
and
coiled
(1,4)
amylopectin =>
branched
and
both
bonds
Cellulose
:
beta
glucose
1,4
glycosidic
bonds
long
parallel
straight chains
linked by hydrogen bonding to form
macrofibrils
provides strength to
cell wall
Lipids examples:
triglycerides
and
phospolipids
Triglycerides
:
formed from a
condensation
reaction between one glycerol and three
fatty
acids
ester
bonds
R group of fatty acids may be
saturated
(single bond) or
unsaturated
(double bond)
Energy storage
due to large ratio carbon-hydrogen bonds
Metabolic water source
as releases water if oxidised due to hydrogen:oxygen
Hydrophobic
so doesn't affect water potential
Phospholipids
:
Made of 2 fatty acids and
one
phosphate
Hydrophyllic
head and
hydrophobic
tail
Used in
cell surface membrane
Insoluble
in water
What is the test for lipids?
Emulsion
test: Mix sample in
ethanol
, add water and a white emulsion should form
Amino acids:
monomers
of proteins
amino acids only differ in their
side chain
/
R
group
peptide
bond forms between
amine
group and carboxyl group
Describe
the structure of proteins?
1.Amino acids are joined by peptide bonds through
condensation
2. Primary structure is the
specific sequence
of amino acids
3. Secondary structure is the
folding
of the polypeptide chain due to
hydrogen bonding
(beta pleated or alpha helix)
4. Tertiary structure is
3D
folding due to
hydrogen
, ionic bonds and disulfide bridges
5. Quaternary structure is
2
or more
polypeptide
chains
What is the test for proteins?
Biuret
test: add
biuret
solution and shake, a positive test will turn from light blue to lilac
What is an enzyme?
a protein that
catalyses
a reaction by
lowering
the activation energy
globular
proteins: compact and water soluble (enzymes/metabolic reactions)
fibrous
proteins: long, insoluble and useful for structure
Factors affecting rate of reaction catalysed by enzymes:
pH
temperature
enzyme
and
substrate
concentration
Competitive inhibition:
inhibitor
similar shape to substrate so binds to
active site
inhibition
can be overcome by adding more
substrate
Non
-competitive inhibitors:
Inhibitors bind to enzyme on
allosteric
site which changes
shape
of active site
cannot be
overcome
DNA and RNA are polymers of nucleotides.
Nucleotide structure:
A)
phosphate group
B)
pentose sugar
C)
nitrogenous base
3
Semi-conservative replication:
Helicase
unwinds double helix by breaking weak
hydrogen
bonds
Each strand is used as a
template
New
DNA nucleotides
are attracted to exposed bases on
parent
strand
DNA polymerase
joins adjacent nucleotides by
condensation
by forming phosphodiester bonds
ATP:
structure : adenine, ribose and
3
phosphate groups
releases
small
amounts of energy
instantaneously
phosphorylates
other compounds to make them more reactive
rapidly
resynthesised
not
lost
from cells
Describe
the 5 properties of water:
Metabolite
=> in condensation/hydrolysis reactions
Solvent
=> allows transport of substances
High
SHC => buffers changes in temperature
Large
latent
heat of vaporisation => provides cooling effect through evaporation
Cohesion
between molecules => supports columns of water in plants
What
does the immune system detect?
Pathogens
,
abnormal body cells
, cells from other organisms and toxins
Antigens
: proteins found on surface of cells which signals to
immune system
if it is non-self
Phagocytosis
:
Debris released by pathogen is detected by
phagocyte
Phagocyte
changes shape and
engulfs
pathogen
Pathogen contained in
phagosome vesicle
Lysosome fuses with vesicle; releasing
enzymes
which
hydrolyses
it
Antigens
on pathogen displayed on
cell membrane
Describe the cell mediated response?
Helper
T
cells receptors attach to antigens on APC
T cells
divide by mitosis
Clones differentiate into
helper T cells
,
cytotoxic
and
memory
T cells
Cytotoxic cells release
perforin
, which makes
pores
in the cell membrane so
water
moves in and the cell bursts
Describe
the Humoral response
B cell binds to
complementary
antigen and
engulfs
it (
endocytosis
) and presents antigen on cell surface
Complementary
T
cell binds to
B cell
B cell goes through
clonal
expansion
to produce plasma and memory cells
Plasma
cells produce antibodies
Antibodies clump together cells through agglutination to form antigen-antibody complexes
This makes it easier for phagocytes to detect
How many polypeptide chains are antibodies made of?
4
Antibodies have
2 binding
sites so they can clump
cells
together
Antibodies have strong disulfide bridge to hold polypeptides together and hinge region so it can bend
Antibody structure:
Heavy
and light chains
constant
region and variable region
What
is the function of the golgi?
Packages and
modifies
proteins
Active immunity:
Body produces it's own antibodies so long term
What is a
mutation
?
Change in the
base sequence
of
DNA
which occurs spontaneously during DNA replication
What
are the types of mutations?
Addition
,
Deletion
and substitution
Not all substitution mutations result in a change of amino acids as genetic code is degenerate
Mutations in number of chromosomes arises by chromosome
dysjunction
during meiosis so chromosomes don't
separate
properly
Meiosis:
produces
4
genetically
different
cells
haploid
number of chromosome combos is
2
to the power of n
split into
2
divisions
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