Why is Carbon the base of life ?
As it can make 4 bonds with elements like H , O and N
Monomer
A molecule that can combine with others of the same kind to form a polymer.
condensation reactions
Chemical process in which two molecules combine to form a more complex one with the elimination of a simple substance, usually water.
Hydrolysis
The breaking down of large molecules into smaller ones by the addition of water molecules .
What are 3 types of carbohydrates ?
Monosaccharides
Disaccharides
Polysaccharides
How many carbons can monosaccharides contain ?
3-7 :
Triose
Pentose
Hexose
2 examples of pentoses
Ribose
Deoxyribose
3 examples of hexoses
Glucose
Fructose
Galactose
3 examples of disaccharides
Maltose
A
Sucrose
A
Lactose
A
what are the 3 non-reducing sugars ?
Cellulose
Starch
Sucrose
what are 3 types of polysaccharides ?
Starch
Glycogen
Cellulose
Starches can be either :
Amylose
or
Amylopectin
Cellulose : features
Straight , long , unbranched , layered and bonded by H-Bonds :
plant based
ß Glucose
(1-4) Bonding
NOT Branched
structural function
not soluble
Amylose : features
Unbranched and coiled :
Plant based
α Glucose
(1-4) Bonding
NOT Branched
Helical
Storage Function
Soluble
Starch it is
Amylopectin : features
Long , branched and sometimes coiled :
Plant based
α Glucose
(1-4) and (1-6) Bonding
Branched (per 20 subunit)
Storage Function
Not soluble
Glycogen : Features
Short , highly branched and sometimes coiled :
Animal based
α Glucose
(1-4) and (1-6) bondings
highly branched ( per 10 subunit )
Storage function
Mostly soluble
Benedict’s test for monomers :
add the food sample to water and grind it up
add Benedict’s reagent
buffer solution for low pH and heat
if turns brownish-red —> reducing sugar is present
Reducing sugar
Sugars capable of donating electrons to other chemicals.
Benedict’s test for disaccharides :
first apply Benedict’s test to prove there’s no reducing agent present.
add HCl to cover disaccharides into monomers.
add sodium hydrogencarbonate ( a base ) to bring the solution back to alkalinity.
reapply the test and prove that this time reducing agents are present!
Isomer
Compounds that have the same molecular formula but different structures.
what type of glucose is this?
Alpha Glucose
Glucose : Features
Highly soluble
Blood sugar it is
the first sugar used in humans in order to produce energy
controlled by insulin and glucagon
produces in plant cells
what type of glucose is this?
Beta Glucose
fructose : features
fruit sugar
plants produce it
humans can turn it into glucose
sweetest sugar
glucose + glucose —>
glucose + fructose —>
glucose + galactose —>
Maltose ( malt sugar )
Sucrose ( table sugar )
Lactose ( milk sugar )
chemical test for the presence of starch
Iodine / Potassium Iodide
if turns black —> (+)
3 types of lipids
triglycerides
waxes
phospholipids
lipids : features
insoluble in water
soluble in non-polar material like acetone, chloroform and alcohols
proportion of O to C and H is less relatively
used as energy source ( 2x of what carbs give away )
waterproof
bad conductors of heat
name the parts :
glycerol
fatty acids
—>
triglyceride
(+ 3 water )
how many types of fatty acids are there
more than 70
saturated fatty acids
no double bond between carbons
unsaturated fatty acids
containing double bonds between fatty acids
( this results in bending of the molecule thus they are found as liquids in nature )
name the parts of a phospholipid
Emulsion test
add lipid to ethanol
mix
add water
if turns cloudy white —> (+)
name the parts
the bondings in the secondary structure :
H bonding :
( between carboxyl and amino groups )
the bondings in the tertiary structure :
disulfide bonds —> R groups
hydrogen bonds —> amine groups, alcohol groups, and acids
ionic bonds —> two side and r groups
prosthetic group
non-peptide (non-protein) compounds that mostly attach to proteins and assist them in different ways.
primary structure
the sequence of aa’s that makes up the polypeptides of a protein
secondary structure
the way in which the chain of aa’s of the polypeptides of a protein are folded ( via H-Bonds )
tertiary structure
the folding of a polypeptide chain in a precise way as determined by the aa of which it is composed .
Quatendary structure
a number of polypeptide chains linked together and smt associated with non-protein groups to form a protein.
peptide bond
the chemical bond formed between 2 aa’s during condensation .
active site
a group of aa’s that makes up the region of an enzyme into which the substrate fits in order to catalyze a reaction .
Biuret test
to find proteins
(+) —> lilac
(— )—> blue
covalent bond
a type of intramolecular bond in which atoms share a pair of electrons , one from each atom .
denaturation
permanent changes due to the unravelling of the 3-d structure of a protein as a result of factors such as TEMP change or pH change .
enzyme
a protein or RNA that acts as a catalyst and so alters the rate of reaction .
H-bond
the chem. bond formed between the positive charge on a H atom and negative charge on a another atom of an adjacent molecule .
Ions
a group of atoms that have lost or gained one or more electrons .
isotope
variations of a chemical element that have the same number of protons while having different numbers of neutrons thus having different masses !
mono-unsaturated fatty acid
FA that possesses a carbon chain with a single double bond
oxidation
loss of electrons
reduction
the gain of electrons
polyunsaturated FA
FA that possesses carbon chains with many double bonds .
Key and Lock theory of enzymes
The lock and key model is a theory of enzyme action that explains how enzymes fit their substrate. The active site of an enzyme is structured to fit a specifically shaped substrate. Once the substrate binds to the active site, the enzyme will facilitate the reaction and release products of the reaction.
induced fit model of enzymes
The induced-fit model states a substrate binds to an active site and both change shape slightly, creating an ideal fit for catalysis. Enzymes promote chemical reactions by bringing substrates together in an optimal orientation, thus creating an ideal chemical environment for the reaction to occur.
competitive inhibitor
blocks the active site ( compete for it )
non permanently bonds with AS
when the substrate conc increase , it’s effects decrease
non-competitive inhibitor
binds the allosteric site
distort the AS
permanent
the difference alpha and beta glucose
the position H and hydroxyl groups on the carbon atom 1 is inverted !
cellulose adaptations
Beta glucose
form long, unbranched, straight sheets
layered
interact and connected by H-Bonds
Microfibrils
provide strength, steardiness and rigidity
starch adaptations
compact
helical
insoluble ( so does not affect the water potential )
hydrolysis lasts shorter than of the cellulose’s
( faster delivery of energy )
ES complex
the temporary molecule made when substrate bonded to enzyme .
the affect of pH on protein
ph low
H+ high
ionic bonds disrupted
tertiary structure broken
Amino acids in enzymes
The monomers that make up the active site ( or the whole molecule )
Triglycerides are Monomers/Polymers
Monomers as they ( themselves ) have got no monomer or repeating smaller units !
PH probe e
A pH meter is a scientific instrument that measures the hydrogen-ion activity in water-based solutions, indicating its acidity or alkalinity expressed as pH .
Why not all enzymes fit all substrates ? (3p)
specific AS due to their specific 3-D structure
Only some of the proteins have complementary shapes to these AS ( not fit )
So ES complex is formed between specific types of molecules
Is ther any starch molecule found in the human blood ?
NEIN
Why a change in the DNA changes the type of the enzyme ? (3P)
DNA change results in a different aa sequence
So different bonds formed between aa’s resulting in a different folding .
So eventually the AS changes !