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Biological molecules
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Cards (49)
Monomers
examples
glucose
amino acids
nucleotides
Polymers
examples
starch
cellulose
glycogen
proteins
DNA
RNA
Describe a condensation reaction to create polymers
1. Joining two molecules together
2. Creating a chemical bond
3. Removing water
Describe a hydrolysis reaction to break apart monomers
1. Breaking of a chemical bond between two molecules
2. Involves the use of water
Carbohydrate monosaccharides
glucose
fructose
galactose
Carbohydrate disaccharides
sucrose
maltose
lactose
Carbohydrate polysaccharides
starch
cellulose
glycogen
Alpha
glucose
Hydrogen
atom on top,
hydroxyl
group on bottom of carbon 1
Beta glucose
Hydroxyl
group on top,
hydrogen
atom on bottom of carbon 1
Glycosidic bond
Chemical bond that forms between two
monosaccharides
in
disaccharides
Starch
Glucose
store in plants
Made from
alpha
glucose
Cellulose
Structural strength in
plant cell walls
Made from
beta
glucose
Glycogen
Glucose
store in animals
Made from
alpha
glucose
Highly
branched
structure
Triglycerides
Lipid
with 3 fatty acid chains attached to a
glycerol
molecule
Phospholipids
Lipid with 2 fatty acid chains and a
phosphate
group attached to a
glycerol
molecule
Formation of triglycerides
1. 3
condensation
reactions
2. 3
water
molecules lost
3. 3
ester
bonds formed
Triglycerides
High ratio of
energy-storing
carbon-hydrogen bonds
Can act as
metabolic
water source
Do not affect
water
potential
Phospholipids
Hydrophilic
head, hydrophobic tails
Form a
bilayer
in water
Amino acid
Central carbon,
hydrogen
, amine group,
carboxyl
group, variable R group
Formation of dipeptide
1.
Condensation
reaction
2.
Water
removed
3.
Peptide
bond formed
Formation of
polypeptide
1. Multiple
condensation
reactions
2. Multiple peptide bonds formed
Levels
of protein structure
Primary
Secondary
Tertiary
Quaternary
Primary structure
Sequence of amino acids in
polypeptide
chain
Secondary structure
Folding into
alpha helix
or beta pleated sheet, held by
hydrogen bonds
Tertiary
structure
Further folding into unique
3D
shape, held by
ionic
, hydrogen and disulfide bonds
Quaternary
structure
Multiple
polypeptide
chains in a single
protein
Enzymes
Proteins in tertiary structure
Catalyze
reactions by
lowering activation energy
Have specific
active sites complementary
to
substrates
Induced fit model
Enzyme active site slightly changes shape to
mold
around
substrate
Factors
affecting enzyme-controlled reaction rate
Temperature
pH
Substrate
concentration
Enzyme
concentration
Inhibitors
Lower
temperature
Less kinetic energy, fewer successful
collisions
, fewer
enzyme-substrate complexes
, lower reaction rate
pH
away from optimum
Enzyme
denaturing
, loss of active site shape, fewer
enzyme-substrate
complexes, lower reaction rate
Increasing substrate concentration
More
collisions
, more
enzyme-substrate
complexes, higher reaction rate until active sites saturated
Increasing
enzyme concentration
More
active
sites available, higher reaction rate until substrate becomes
limiting
Competitive
inhibitor
Binds to
active site
,
preventing
substrate binding
Non
-competitive inhibitor
Binds
elsewhere on enzyme, changing active site
shape
Competitive
inhibitor
Binds to the
active site
of an enzyme,
preventing
the substrate from binding
Non
-competitive inhibitor
Binds to the
allosteric
site of an enzyme, changing the
shape
of the active site and preventing the substrate from binding
Biochemical
test for starch
1. Add
iodine
2. Positive test result:
iodine
goes from orangey brown to
blue black
Biochemical test for reducing sugars
1. Add
Benedict's
reagent and
heat
2. Positive test result: solution turns green, yellow, orange or
brick red
(depending on
concentration
)
Biochemical
test for non-
reducing
sugars
1. Perform
Benedict's
test for
reducing
sugars (negative result)
2. Add
acid
and
boil
3.
Cool
and
neutralise
4. Add
Benedict's
reagent and
heat
5. Positive test result: solution turns
orange
or brick red
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