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Cards (262)
Monomers
are
smaller
units which can create larger molecules and the polymers are made from lots of monomers which are bonded together
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Monomers
glucose
amino
acids
nucleotides
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Polymers
starch
cellulose
glycogen
proteins
DNA
RNA
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Condensation reaction to create
polymers
1. Joining two
molecules
together
2. Creating a
chemical
bond
3. Removing
water
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Hydrolysis reaction to
break apart
monomers
1. Breaking a
chemical
bond between two molecules
2. Involving the use of
water
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Carbohydrate monosaccharides
glucose
fructose
galactose
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Carbohydrate disaccharides
sucrose
maltose
lactose
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Carbohydrate polysaccharides
starch
cellulose
glycogen
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Alpha
glucose
Hydrogen
atom on top,
hydroxyl
group on bottom of carbon 1
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Beta glucose
Hydroxyl
group on top,
hydrogen
atom on bottom of carbon 1
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Glycosidic bond
Chemical bond that forms between two
monosaccharides
in disaccharides and
polysaccharides
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Starch
Glucose
store in plants
Alpha
glucose monomers
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Cellulose
Structural
strength in plant cell walls
Beta
glucose monomers
One-to-four
glycosidic bonds
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Glycogen
Glucose
store in animals
Alpha
glucose monomers
One-to-four
and
one-to-six
glycosidic bonds
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Triglycerides
Lipid
with three fatty acid chains attached to a
glycerol
molecule
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Phospholipids
Lipid
with two fatty acid chains and a
phosphate
group attached to a glycerol molecule
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Saturated fatty acid
No
double
bonds between carbon atoms, fully saturated with
hydrogen
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Unsaturated fatty acid
At least one
double
bond between
carbon
atoms
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Triglycerides
High ratio of
energy-storing
carbon-hydrogen bonds
Can act as
metabolic
water source
Do not affect
water potential
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Phospholipids
Hydrophilic
head,
hydrophobic
tails
Form a
bilayer
in water
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Amino acid
Central carbon,
hydrogen
, amine group,
carboxyl
group, variable R group
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Forming a
dipeptide
Condensation
reaction to remove water and form a
peptide
bond
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Forming a
polypeptide
Multiple
condensation
reactions to form
peptide bonds
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Primary protein structure
Order or sequence of amino acids in a
polypeptide
chain
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Secondary protein structure
Folding
or twisting of the polypeptide chain, held by
hydrogen
bonds
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Tertiary
protein structure
Further
folding
to create a unique
3D
shape, held by ionic, hydrogen and disulfide bonds
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Quaternary protein structure
Protein made up of more than one
polypeptide
chain
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Enzyme
Protein
in the tertiary structure that catalyzes reactions by
lowering activation energy
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Enzymes
Specific to one reaction due to unique active site
shape
Work by
induced fit
model - active site changes
shape
to fit substrate
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Factors affecting enzyme-controlled reaction rate
Temperature
pH
Substrate
concentration
Enzyme
concentration
Inhibitors
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Competitive inhibitor
Binds to the
active site
of an enzyme
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Non-competitive
inhibitor
Binds to a
different
part of the enzyme
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Competitive inhibitor
Binds to the
active site
of an enzyme,
preventing
the substrate from binding
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Non-competitive inhibitor
Binds to the
allosteric
site of an enzyme, changing the
shape
of the active site and preventing the substrate from binding
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Biochemical test for starch
1. Add
iodine
2. Positive test result:
iodine
goes from orangey brown to
blue black
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Biochemical test for reducing sugars
1. Add
Benedict's
reagent
2.
Heat
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Biochemical test for non-
reducing
sugars
1. Do
Benedict's
test for
reducing
sugars
2. If negative, add
acid
and
boil
3.
Cool
and
neutralise
4. Add
Benedict's reagent
again
5.
Positive
test result: solution turns
orange
or brick red
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Biochemical test for proteins
1. Add
biuret
reagent
2. Positive test result: solution turns
purple
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Biochemical test for lipids
1.
Dissolve
sample in
ethanol
and shake
2. Add
distilled
water
3. Positive test result:
white emulsion
forms
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DNA
Contains the
genetic
code and can be passed on to make new
cells
and to the next generation
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