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Title: Biological molecules
Description: A detailed explanation of biological molecules. Suitable for O/A level and 1st year med students
Description: A detailed explanation of biological molecules. Suitable for O/A level and 1st year med students
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Topics 1-4: Biological molecules
Lipids
Made
of
Bonds
Prope
rties
S&F
Insoluble in water
High solubility in non-polar solvents
Simple lipids, compound lipids, and lipid derivatives
Non-polymer
Simple Lipid
(triglycerides)
Glycerol
3 fatty acids
Compound Lipid
(phospholipids)
Esters of 2 fatty acids
An alcohol
Additional small charged
group (eg choline, serine)
Ester linkage btw OH
Ester linkage; phosphoester
group of Glycerol and
linkage btw 3rd OH group of
COOH group of a fatty
glycerol and phosphate
acid by condensation
group
Melting point
Amphipathic
increases with
Aggregate in aqueous
hydrocarbon chain
environment to shield
length and degree of
hydrophobic tails from
saturation
water
Saturated fats (no
Micelle: small, spherical
double bonds)
droplet; monolayer
Unsaturated fats
Bilayer: 2D sheet
(contains double
Liposome/vesicle: hollow
bonds)
sphere formed when
bilayer folds back on itself
Structure
Function
Structure
Function
Hydrophobic Allow motile Amphipathic Forms a
organisms hydrophobic selectively
fatty acid;
to keep
permeable cell
their mass hydrophilic
membrane;
phosphate
to a
boundary btw
head
minimum
cell & external
environment
Does not
Liposome/
affect cells’
water
vesicle:
potential
storage and
transport of
Good
cellular
thermal
products
insulator
Micelles:
transport fats
Weak
Adipose
Hydrophobic Maintain
hydrophobic tissue
interaction
integrity of
interaction cushions & btw fatty
membrane
protects
acid tails
bilayer
Compound Lipid (glycolipids)
Glycerol
2 hydrocarbon tails
A polar, short
carbohydrate chain
Glycosidic bond btw OH
group of glycerol and C atom
on carbohydrate chain
Amphipathic due to
soluble carbohydrate
chain and insoluble
hydrocarbon tails
Structure
Carbohydra
te chain
attached to
lipid
Hydrocarbo
n tails
Function
Found on cell
surface
membrane
facing
external
environment
Serves as a
marker in
cell-cell
recognition
Involves in
cell-cell
adhesion as
a result of
binding
Hydrophobic
interaction
btw fatty acid
tails serve to
Topics 1-4: Biological molecules
vital organs
anchor the
Permit lateral
against
glycolipids at
movement:
physical
cell surface
membrane
impact
membrane
fluidity
Lower
Aid
Contain
Important for
density than buoyancy of choline
synthesis of
water
aquatic
acetycholine
animals
Higher
Efficient
proportion energy
of C and H to store:
O atoms
releases
38kJ/g upon
oxidation
Large
Release
number of C- metabolic
H bonds
water
Kink: a bend in the hydrocarbon chain caused by a C=C double bond; prevents the molecules from
packing closely enough, thus weakening hydrophobic interactions and lowering the melting point
Lipid derivative: eg
...
Intercalated in
phospholipid membrane; interferes in hydrophobic interactions
...
Starch
and glycogen)
Serve as structural
materials (eg
...
Proline: bulky aa residue; does not fit readily into secondary
structure, producing kinks Cysteine: forms strong covalent disulphide bridge with another
cysteine aa residue
...
collagen,
haemoglobin
• Ionic, Hydrogen,
disulfide bonds and
hydrophobic
interactions
Topics 1-4: Biological molecules
α-helix
Extended spiral spring (3
...
Topics 1-4: Biological molecules
Enzymes lower activation energy by:
1
...
Straining critical bonds in the substrate molecule(s), allowing the substrates to attain
their unstable transition state configuration
3
...
Name limiting factor
2
...
Frequency of effective collision between
E and S
4
...
Rate of formation of products
Temperature:
1
...
3
...
Change in kinetic energy of E and S
Frequency of effective collisions btw E and S
Rate of formation of E-S complex
Likeliness of over activation energy barrier
1
...
Less/more H+ ions to neutralise negative
charges present in enzyme
3
...
Denaturation
5
...
Rate of formation of products
6
...
At high [S], S can out-compete I
Effect on Km increase
Non-competitive Inhibition
Structurally not similar to substrate
Any other part, alters 3D conformation of E
Decrease in [E]
Decrease
Same
Allosteric regulation:
Usually occurs in multi-subunit enzymes
Regulation of an enzyme by the binding of molecules at an allosteric site
Activators stabilise the active form of the enzyme, increasing the affinity of E for S
Inhibitors binds to the same region, stabilizing the inactive form of the enzyme, and
decreasing the affinity of E for S
Control and Regulation of Metabolic Pathways
Controlled by multi-enzyme complex
o Biological reactions may proceed with no accumulation of products in cells, as
products become substrates of subsequent reactions
o Reactants are modified in series of small steps enabling controlled release of energy
and minor adjustments to be made to molecules
o Each step is catalysed by a specific enzyme, so each enzyme act represents a point
of control of the overall pathway
o Spatially arranged so that product of one reaction is ideally located to become the
substrate of the next enzyme, permitting the build up of high local [S] and
biochemical reactions can proceed rapidly
o Sequencing of reactions greatly increase the efficiency of the enzyme pathway
End-product inhibition is when accumulation of end-products act as inhibitors on the
enzyme(s) controlling the preceding step(s) of the pathway
Title: Biological molecules
Description: A detailed explanation of biological molecules. Suitable for O/A level and 1st year med students
Description: A detailed explanation of biological molecules. Suitable for O/A level and 1st year med students