MEMBRANE BIOCHEMISTRY

Structure, characteristics
Functions for transport, signal transduction
reaction

Maggy T. Suhartono
Bogor Agricultural University

Dedicated to Prof. Richard J Guillory of University of Hawaii Manoa who

introduced me to a fascinating membrane biochemistry
The boundaries of cells =
Biological membranes
(barriers that define the
inside and outside of a cell).

Prevent molecules leaking out

and unwanted molecules from
diffusing in.

Allow the cell to take up

specific molecules and remove
unwanted ones.

Internal membranes :
mitochondria, chloroplasts,
peroxisomes, lysosomes
 MEMBRANE STRUCTURE

Membrane structure : Bilayer, dynamic, asymetric

Main component : phospholipid, protein
Other component : substances dissolved in membrane
(cholesterol, chlorophyl, vitamine, triglyserida, wax, etc.)
 Membrane Protein : integral, peripheral
Movement of membrane : lateral, not flip-flop
For glycolipid and glycoprotein, the sugar reside outside
MEMBRAN
Common features and diversity of membranes

1. Membranes are sheetlike structures, only two molecules

thick (60~100)
2. Membranes consist of lipids and proteins.
3. Membrane lipids are small molecules that have both
hydrophilic and hydrophobic moieties.
4. Specific proteins mediate distinctive functions of
membranes (pumps, channels, receptors, energy and
signal trasnducers and enzymes).
5. Membranes are noncovalent assemblies.
6. Membranes are asymmetric.
7. Membranes are fluid structures.
8. Most cell membranes are electrically polarized.
 Membrane Proteins

Peripheral proteins
Associate with
membrane surface
(lipids or protein)
Can be dissociated by
changes in solution
conditions (salt, pH)
Integral proteins
Interact with
hydrophobic bilayer
core
Membrane Spanning
Lipid Anchors
- Example : peripheral protein Lies along outer surface of the membrane
firmly bound by a set of helices with hydrophobic surfaces that
extend from the bottom of the protein into the membrane.

- Partially embedded.
Amphipathic membrane
detergents :
required for
solubilization of detergent polar
integral proteins solubilization non-polar
from membranes.

Protein with
bound detergent

Hydrophobic domains of detergents substitute for lipids, coating

hydrophobic surfaces of integral proteins.
Polar domains of detergents interact with water.
If detergents are removed, purified integral proteins tend to
aggregate & come out of solution. Their hydrophobic surfaces
associate to minimize contact with water.
Membranes contain specialized lipids and proteins

Proteins 30-70%
Phospholipids 7-40%
Sterols 0-25%
Specialized membranes
More than 90% Rhodopsin
in photoreceptor disc
membrane
Protein rich mitochondrial
membranes
Transport optimized Red
Blood Cell membrane
All biological membranes : asymmetric
-Structurally and functionally asymmetric.
-Different component and enzymatic activity between outer
and inner membrane.

Na+ - K+ PUMP
-Na+ out of the cell.
-K+ into the cell.
 Membran protein :
Characteristics and examples
 Proteins carry out most membrane processes

-Specific proteins mediate membrane functions.

-Membranes differ in their
protein contents.
- Membranes contains many
proteins, but has a distinct
protein composition.
 A channel protein can be formed from beta strands
-Porin : built from strands and no helices.
-Each strand is H bonded to its neighbor in an antiparalle arrangement.
-The outside surface of porin is nonpolar. Interact with the hydrocarbon
chains.
-The inside of the channel is hydrophilic and filled with water.
-Alternation of hydrophobic and hydrophilic amino
acids along each strand. Why?
-Hydrophobic yellow
 Proteins can span the membrane with alpha helices

-Bacteriorhodopsin : uses light energy to transport protons from inside

the cell to outside proton gradient.
-Almost helices; 7 closely packed helices.
-Span its 45 width.
-Examination of primary structure of bacteriorhodopsin :
most of the amino acid in helices are nonpolar(yellow) and
only a very few are charged(red).

-Membrane-spanning helices are the most common

structural motif in membrane proteins.
- Prostaglandin H2 synthase-1 : catalyzes conversion of
arachidonic acid into prostaglandin H2 in two steps.

1. Cyclooxygenase reaction

2. Peroxidase reaction

- Prostaglandin H2 promotes
inflammation and modulates
gastric acid secretion
- Location of prostaglandin H2 synthase-1 in membrane is crucial to its
function.
-Substrate (arachidonic acid) : hydrophobic, generated by hydrolysis of
membrane lipids.
-Substrate reaches active site through a hydrophobic channel (yellow).
-Drug (aspirin) block the channel.
alanine (Ala, A) isoleucine (Ile, I) leucine (Leu, L) valine (Val, V)
H H H H

H3N+ C COO H3N+ C COO H3N+ C COO H3N+ C COO

CH3 CH CH3 CH2 CH CH3

CH2 CH CH3 CH3

CH3 CH3
amino acids: non-polar aliphatic R-groups

Particular amino acids tend to occur at different positions relative

to the surface or interior of the bilayer in transmembrane segments
of integral proteins.

Residues with aliphatic side-chains (leucine, isoleucine, alanine,

valine) predominate in the middle of the bilayer.
 tryptophan tyrosine
H H

Tyrosine and H2N C COO H3N+ C COO

tryptophan are
common near the CH2 CH2

membrane
surface.
HN

OH

Polar character of the tryptophan amide group and the

tyrosine hydroxyl, along with their hydrophobic ring
structures, suit them for localization at the polar/apolar
interface.
 lysine arginine
H H

H3N+ C COO H3N+ C COO

CH2 CH2

CH2 CH2

CH2 CH2

CH2 NH

NH3 C NH2

NH2

Lysine & arginine often at the lipid/water interface, with

the positively charged groups at the ends of their
aliphatic side chains extending toward the polar membrane
surface.
 Sequence predictions of
Membrane spanning domains
Hydropathy plots
average hydrophobicity over N
successive residues (N=7-20)
alpha helix dimensions 3.6
residues/turn over 5.4
Angstroms
Bilayer dimensions ~30
Angstroms / 5.4 = ~6 turns of
helix or 21 AAs
Hydrophobic stretches of ~20
residues are often membrane
spanning helices

7-9 residues of (more extended)

beta strands can span the
membrane
 Glikoprotein Glikolipid

Bagian karbohidrat glikoprotein terikat pada hidroksil (ikatan O) serin

/threonin atau pada amida (ikatan N) aspargin protein ybs
Glikoforin : glikoprotein pada membran sel darah merah, protein integral :
gula/karbohidrat sampai 60 %, Jumlahnya 2 % total berat protein
membran. Berfungsi mencegah pengggumpalan karena mengandung asam
sialat bermuatan negatif, sebagai pembeda golongan darah dan reseptor
virus
Membrane
fluidity support
dinamic
activities,
The fluid mosaic model allows lateral movement but not
rotation through the membrane
 Lateral diffusion may be limited by protein networks

Cytoskeletal
connections
or
membrane
patches
 Lateral diffusion

Lipids and proteins can

diffuse in 2D
Measured by Fluorescence
Recovery After Photo-
bleaching FRAP
FRAP requires fluorescent
tag on lipid or protein

Photobleaching of a small
area by intense light pulse
makes a dark spot
Recovery depends on
diffusion of undamaged
fluorophores to the
bleached spot
Lipids and many membrane proteins diffuse rapidly in the
plane of the membrane
-Lateral diffusion : lipids and many membrane proteins are
in lateral motion.
- FRAP(fluorescence recovery after photobleaching)
1. Cell-surface component is labeled with a fluorescent chromophore.
2. A small region is viewed through a fluorescence microscope.
3. Fluorescent molecules in this region are destroyed by laser.
4. This region is monitored.
5. Bleached molecules leave and unbleached molecules enter.
6. Recover the fluorescent intensity in this region.
-The rate of recovery depends on the lateral mobility of
the component, which can be expressed in terms of a
diffusion coefficient, D.
-The average distance S = (4Dt)1/2
-Rhodopsin s D = 0.4m2/s
-Fibronectins D = 10-4m2/s (because it is anchored to
actin filaments on the inside of the plasma membrane
through integrin.)
-The lateral diffusion can be rapid.

-The transition of a molecule from

one membrane surface to the other
is very slow = transverse diffusion
or flip-flop.
 Flip Flop
Flip-flop require the polar head-group of a lipid to traverse
hydrophobic core of the membrane.

Flippases catalyze flip-flop in membranes where lipid synthesis occurs.

Some membranes contain enzymes that actively transport particular
lipids from one monolayer to the other.
 Transbilayer
transport by
flippases

Barriers to
transbilayer
lipid movement
are high

Lipid
biosynthesis on
one side of a
membrane is
coupled to
catalyzed
transport
 Three common types of membrane lipids

1.Phospholipids
2.Glycolipids
3.Cholesterol

Lipids have a variety of biological roles :

1.Components of membranes.
2.Fuel molecules.
3.Signal molecules and messengers in signal transduction.
What is the difference between phospholipid and and
triglyseride?

Why triglyseride is not suitable as main component of

membrane?
Membrane fluidity is controlled by fatty acid composition
and cholesterol content

-Membrane transport or signal transduction depend to the

fluidity of the membrane lipids.

- The transition from rigid to

the fluid state takes place
rather abruptly as the
temperature is raised above
Tm, the melting temperature.
Fatty acids vary in chain length and degree of unsaturation

-16~18 carbon fatty acid are most common.

-The properties of fatty acid and of lipids derived from them are
dependent on chain length and degree of saturation.
Unsaturated fatty acid = lower melting points
saturated fatty acid = higher melting points (same length)
number starting at the carboxyl
terminals.
-Carbon atom 2 =
-Carbon atom 3 =
-Methyl carbon atom at the distal
end of the chain = -carbon atom

-Position of double bond =

-Ex> cis-9 = cis double bond
between carbon 9 and 10.

-Double bond counting from the

distal end = -carbon as number1.
-Ex> -3
-Tm depends on the length of the fatty acid chains and on
degree of unsaturation.
-A cis double bond produces a bend in the hydrocarbon
chain. This bend interferes with a highly ordered packing
of fatty acid chains, and so Tm is lowered.
Lipid
separation
and analysis
Phospholipids the major class of membrane lipids

-One or more fatty acids

-Platform to which the

fatty acids are attached

-Phosphate

-alcohol

-Phospholipids are abundant in all biological membranes.

- Composed with 4 components.
-Platform are built may be glycerol, a three carbon alcohol, or
sphingosine.
Phospholipid is the main component due to their
amphiphatic (polar-nonpolar) characteristics
Hydrophobic C chain hidrophobic interaction
Charge substances / chain electrostatic interaction
-Phosphoglyceride : phospholipid derived from glycerol.
-C1 and C2 are esterified to the carboxyl groups of the two
fatty acid chains.
-C3 hydroxyl group is esterified to phosphoric acid.

-When no more addition the simplest fatty acid,

phosphatidate
 Phosphatidate
O

O H2C O C R2

R1 C O CH O

H2C O P O

O
phosphatidate

In phosphatidate:
fatty acids are esterified to hydroxyls on C1 & C2
the C3 hydroxyl is esterified to Pi.
They can be attached
to phosphate group as
alcohol moieties.
 O

O H2C O C R2

R1 C O CH O

H2C O P O X

O
glycerophospholipid

In most glycerophospholipids (phosphoglycerides),

Pi is esterified to OH of a polar head group (X): e.g.,
serine, choline, ethanolamine, glycerol, or inositol.
The 2 fatty acids tend to be non-identical.
They may differ in length and/or the presence/absence of
double bonds.
 O

O H2C O C R2

R1 C O CH O

H2C O P O

O H

OH OH
H OH
OH H
phosphatidyl- H H
inositol H OH

Phosphatidylinositol, with inositol as polar head group, is

one glycerophospholipid.
In addition to being a membrane lipid,
phosphatidylinositol has roles in cell signaling.
 O

O H2C O C R2

R1 C O CH O CH3
+
H2C O P O CH2 CH2 N CH3

O CH3

phosphatidylcholine

Phosphatidylcholine, with choline as polar head

group, is another glycerophospholipid.
It is a common membrane lipid.
 Membrane lipids can include carbohydrate moieties
-Glycolipid : sugar containing lipid.
-Derived from sphingosine.
-Amide group is acylated by a fatty acid.

-Primary hydroxyl group is linked to one or more sugars.

-Sugar residues always on the extracellular side of the

membrane.
Two strategies by which phase changes of membrane
lipids are avoided:

Cholesterol is abundant in membranes, such as plasma

membranes, that include many lipids with long-chain
saturated fatty acids.

In the absence of cholesterol, such membranes would

crystallize at physiological temperatures.

The inner mitochondrial membrane lacks cholesterol,

but includes many phospholipids whose fatty acids have
one or more double bonds, which lower the melting
point to below physiological temperature.
-Bacteria regulate fluidity of their membranes by varying the number
of double bonds and length of fatty acid chains

-In animals, Cholesterol is the key regulator of membrane fluidity,

-Cholesterol disrupts the interactions between fatty acid chain

increasing the membrane fluidity.
-Cholesterol forms specific complexes with some phospholipids to make
lipid rafts
Cholesterol is a lipid based on a steroid nucleus

Hydrocarbon

Hydroxyl group

-Only found in virtually all animal membranes.

-Almost 25% of the membrane lipids in nerve cell.
-Absent from some intracellular membranes.
Cholesterol, an
important
constituent of cell
membranes, has a
rigid ring system and
a short branched HO
hydrocarbon tail. Cholesterol

Cholesterol is largely
hydrophobic.
But it has one polar group,
a hydroxyl, making it
amphipathic.

PDB 1N83 cholesterol

 HO Cholesterol
Cholesterol in membrane

Cholesterol inserts into bilayer membranes with its

hydroxyl group oriented toward aqueous phase &
its hydrophobic ring system adjacent to fatty acid
chains of phospholipids.
The OH group of cholesterol forms hydrogen bonds
with polar phospholipid head groups.
 Archaeal membranes are built from ether lipids with
branched chains
-differ from
eukaryotes or
bacteria membranes.
1.Nonpolar chains joined
to a glycerol backbone by
ether than ester linkages
(ether is more resistant to
hydrolysis)

2.Alkyl chains branched

(branched chain is more
resistant to oxidation)

3.Stereochemistry of the
central glycerol is inverted.
 Lipid vesicles can be formed from phospholipids

-Lipid vesicles, or liposomes are aqueous compartments

enclosed by a lipid bilayer.
-Can be used to study membrane permeability or to deliver
chemicals to cells.
-Liposomes formed by suspending
a suitable lipid, such as
phosphatidylcholine , in an aqueous
medium.

-Sonicating

-Vesicles formed.(diameter of
about 500)
-Ions or molecules can be trapped
in the vesicles.

-Molecule containing vesicles can

be separated by dialysis or gel
filtration chromatography.
Membrane function : Transport
 Lipid bilayers highly impermeable to ions and most polar
molecules
1/109

-Lipid bilayer membranes have a very low permeability for ions and
most polar molecules. Why?
-Na+ and K+ traverse the membranes 109 times as slowly as does H2O.
 Solute Transport Across Membranes

Simple
Diffusion
Facilitated
Diffusion
Pores,
Channels
Ionophores
Active
Transport
Direct
Coupled
Passive transport - facilitated diffusion by
proteins

Simple diffusion
Rate determined by lipid/aqueous solubility
Driving force is the sum of
Simple chemical potential and
electrochemical potential
Not saturable (no Vmax)

Facilitated Diffusion - "passive transport

Transporters or Permeases are proteins
Directionality determined by concentration and
electrochemical gradients
TRANSPORT

G = RTln(Cin /Cout)

1. Difusi / Osmosis

From high concentration to lower concentration

Does not need energy
For nonpolarand medium size substances
 Aquaporins
Specific channels that allow large amounts of water to move along its
concentration gradient, passive respond to changes in osmotic pressure
Egg cell
2. Passive Transport
# Does not need energy
# Need protein for binding and transport
 conformation conformation
change change

Carrier-mediated solute transport

Carrier proteins cycle between conformations in which a solute binding
site is accessible on one side of the membrane or the other.
There may be an intermediate conformation in which a bound substrate
is inaccessible to either aqueous phase.
With carrier proteins, there is never an open channel all the way
through the membrane.
3. Active Transport

Require energy
Oppose concentration gradient
 Active Transport
Energy coupling can transport against a concentration
gradient

Primary
Transport is
coupled to a
chemical process
(ATP hydrolysis)

Secondary
Transport is
coupled to a
favorable
transport process
Mechanism of Na-K ATPase
3 Na out vs 2 K inside
Require ATP for conformational change
Inhibited by tetrodotoxin
 F-type ATPases - Proton Gradients <==> ATP

Can either use ATP to pump protons or proton gradients to make ATP
 Ion Gradients - Na+ or H+ can drive secondary transport
lac permease - bacterial lactose proton symport
Active transport of Lactose depends on maintenance of proton gradient
 Uniport Symport Antiport
Classes of
carrier A A B A
proteins

Uniport (facilitated diffusion) carriers mediate transport

of a single solute.
An example is the GLUT1 glucose carrier.
The ionophore valinomycin is also a uniport carrier.
 Erythrocyte glucose transporter - Uniport
GlUT1 transports glucose into red blood cells
Specific for glucose, over other sugars
Kinetics of glucose transport into erythrocytes
Cotransport : transport together require binding protein
Counter transport : opposing direction require binding protein

Counter transport
 Chloride-Bicarbonate Exchange - Antiport

Chloride and
Bicarbonate
carry the same
charge
move in opposite
directions - ping
pong mechanism
maintain electro-
neutrality
Cl-in + E <=> E + Cl-out
HCO3-out + E <=> E +
HCO3-in
 mitochondrial
matrix

ATP 4

ADP 3

adenine nucleotide translocase

Example of an antiport carrier:

Adenine nucleotide translocase (ADP/ATP exchanger)
catalyzes 1:1 exchange of ADP for ATP across the inner
mitochondrial membrane. Blocked by Asam Bongkrek
 ABC transporters - homologous family
classified by sequence and structure - not by function
ATP dependent transport
Multidrug resistance transporter pumps out foreign compounds
The chloride channel CFTR responsible for cystic fibrosis
Flippases for transbilayer lipid transport
 Na+- Glucose Symport in human intestine

2 Na+out + Glucoseout -
-> 2 Na+in + Glucosein

Combination of
sodium chemical
potential and
membrane potential

provide driving force

for ~9000 fold
concentration
[Glucose]in/[Glucose]
out
 Protein Channels

Cellular channels usually consist of large protein

complexes with multiple transmembrane a-helices.

Control of channel gating is a form of allosteric

regulation. Conformational changes associated with
channel opening may be regulated by:
Voltage
Binding of a ligand (a regulatory molecule)
Membrane stretch (e.g., via link to cytoskeleton)
 Ion selective channels

Ligand gated
Acetylcholine
Receptor
Neuromuscular
junction

Voltage Gated
K+ Channel
Ligand-Gated Channel Protein Opens in Response to a Stimulus
Transport via Endositosis
# Require receptor
# Example : Cholesterol is transported
into the cell
- Membranes must be able to separate or join together so that cells and
compartments may take up, transport, and release molecules.

- Breaks off and fuses to

form a vesicle.

- The vesicle containing

the LDL fuses with a
lysosome degradation.

- Many cells take up molecules

LDL receptor : recycled.
through the process of receptor-
Cholesterol and amino acid :
mediated endocytosis.
store or use
- Hormones, antibodies, transport
proteins
Iron is essential but Free
iron ions are toxic
because of free radical
formation.

Special transport is
necessary
- The reverse process (the fusion of a vesicle to a membrane)
is a key step in the release of neurotransmitters from a
neuron into the synaptic cleft.
Neurotransmitter release due to vesicle fusion at gap junctions
SNAP - NSF Attachment Protein
SNARE - Soluble NSF Attachment protein REceptor
 Signal transduction

Only cells with the

necessary
receptors can
respond to a
signalthe target
cell must be able to
sense it and
respond to it.
A signal transduction
pathway involves a
signal, a receptor,
and a response.
common mechanism of
signal transduction is
allosteric regulation.
This involves an
alteration in a
proteins shape as a
result of a molecule
binding to it.
A signal transduction
pathway may produce
short or long term
responses.
 A signal molecule, or ligand, fits into a
three-dimensional site on the receptor
protein.

Binding of the ligand causes the

receptor to change its three-
dimensional shape.

The change in shape initiates a cellular

response.
Ligands are generally not metabolized
further, but their binding may
expose an active site on the
receptor.
Binding is reversible and the ligand can
be released, to end stimulation.
An inhibitor, or antagonist, can bind in
place of the normal ligand.
Receptors classified by their activity:
G proteinlinked receptors
Protein kinase receptors
Ion channel receptors
 Some signals activate
adenylate cyclase and use
cAMP as a second messenger
include:
corticotropin, dopamin
epinephrine (b-adrenergic),
follicle-stimulating hormone,
glucagon,
many odorants,
prostaglandins E1and E2,
Ligands binding to G proteinlinked receptors expose a site that can bind
to a membrane protein, a G protein.
The G protein is partially inserted in the lipid bilayer, and partially exposed
on the cytoplasmic surface.
Many G proteins have 3 subunits and can bind 3 molecules: receptor, GDP
and GTP, used for energy transfer and An effector protein to cause an
effect in the cell
Activated G proteinlinked receptor exchanges GDP bound for a higher
energy GTP. and activates effector protein (AC) leading to signal
amplification.
Signaling can initiate a cascade of protein interactionsthe signal can then
be amplified and distributed to cause different responses.
A second messenger is an intermediary between the receptor and the
cascade of responses. In the fight-or-flight response, epinephrine
(adrenaline) activates the liver enzyme glycogen phosphorylase.
The enzyme catalyzes the breakdown of glycogen to provide quick energy.
 The Nobel Prize in
Physiology or Medicine 1994
Signal Transduction in Cells

first messenger (1),

adrenaline, binds specific
receptor (2), Transducer (3),
G protein - composed of
alpha-, beta- and gamma
subunits - is activated.
Stimulates
the amplifier (4), adenylate
cyclase, produces
(5) second messenger, cyclic
AMP, from (6) ATP
(adenosine- triphosphate).
(7) A cascade of enzymatic
reactions alters behaviour of
the cell and
(8) via phosphorylation (9)
glycogen is transformed to
(10) glucose, to generate ATP
.
Phosphorylation can alter
membrane proteins, for
example, ion channels (11).
The second messenger
(cAMP).
Second messengers allow
the cell to respond to a
single membrane event
with many events inside
the cellthey
distribute the signal.
They amplify the signal by
activating more than
one enzyme target.
Phosphodiesterase enzymes
catalyze:
cAMP NH2
cAMP + H2O AMP
Phosphodiesterase is activated by N
N
phosphorylation catalyzed by
Protein Kinase A. N
N

H2 O
Thus cAMP stimulates its own 5' C 4'
H H 1'
degradation, leading to rapid O
H 3'
turnoff of a cAMP signal. P O
2' H
OH
O
O-
 Protein Kinase O

Protein OH + ATP Protein O P O + ADP

O
Pi H2O
Protein Phosphatase

Protein kinase transfers terminal phosphate of ATP to a hydroxyl

group on a protein.
Protein phosphatase catalyzes removal of the Pi by hydrolysis

Protein kinases and phosphatases are regulated by complex signal

cascades.
Some protein kinases activated by Ca++-calmodulin.
Protein Kinase A activated by cyclic-AMP (cAMP).
Protein kinases catalyze
:
ATP + protein ADP +
phosphorylated
protein
Each protein kinase has
a specific target
protein, whose
activity is changed
when it is
phosphorylated.
Signal Transduction Regulatory Mechanisms
 Inhibitionprotein kinase A inactivates glycogen
synthase through phosphorylation, and prevents glucose
storage.
ActivationPhosphorylase kinase is activated when
phosphorylated and is part of a cascade that results in
the liberation of glucose molecules.

Signal transduction ends after the cell responds

enzymes convert each transducer back to its inactive
precursor.
The balance between the regulating enzymes and the
signal enzymes determines the cells response.
 Phosphatidylinositol Signal Cascades

O H2C O C R2

R1 C O CH O

H2C O P O

O H
1 6
OH OH
H OH
2 H 5
OH
phosphatidyl- H H
3 4
inositol H OH

Some hormones activate a signal cascade based on the

membrane lipid phosphatidylinositol.
 O
Different isoforms
O H2C O C R2
of Phospholipase C
have different R1 C O CH O
regulatory domains,
& thus respond to H2C O P O
different signals. O H
cleavage by
A G-protein, Gq Phospholipase C OH
1 6
OPO32
activates one form H OH
of Phospholipase C. 2 OH H 5

H H
PIP2 3 4
phosphatidylinositol- H OPO32
4,5-bisphosphate

When a particular GPCR (receptor) is activated, GTP exchanges for GDP.

Gqa-GTP activates Phospholipase C.

Ca++, which is required for activity of Phospholipase C, interacts with (-)

charged residues & with Pi moieties of the phosphorylated inositol at the
active site.
 OPO32 H
1 6
OH OPO32
H OH O
2 OH H 5
O H2C O C R2
H H
3 4 R1 C O CH
2
H OPO3
IP3 H2C OH
inositol-1,4,5-trisphosphate diacylglycerol
Cleavage of PIP2, catalyzed by Phospholipase C, yields 2
second messengers:
inositol-1,4,5-trisphosphate (IP3)
diacylglycerol (DG).

Diacylglycerol, with Ca++, activates Protein Kinase C, which

catalyzes phosphorylation of several cellular proteins,
altering their activity.
Bacterial Membrane

Peptidoglican : monomer N-asetil

glucosamine (NAG) dan N-asetil
muramic acid (NAM)
 Gr positive Gr negative
Thick murein Thin murein
Eukaryotic cells contain compartments bounded by internal
membranes

Protection

Plasma membrane
Permeability barrier

-Gram negative bacteria (E.coli)

-When staining, pink color
-Double membrane
-Thin cell wall (peptidoglycan)
between them.
-LPS (lipopolysaccharide)
-Small molecules permeable due
to porin
-Gram positive bacteria and
archaea.
-When staining, violet color
-Single membrane surrounded by
cell wall (thick peptidoglycan
layer)
Cell wall
Component : celulose, hemicelulose, lignin
 Plant Cell
Cell wall

Protect and support the enclosed

substances (protoplasm)
Resist entry of excess water into
the cell
Give shape to the cell
A dead layer
Large empty spaces present
between cellulose fibres
freely permeable
 Cell walls
Primary plant cell walls are composed
mainly of carbohydrates and
proteins.

Some cells produce a rigid

secondary wall that
incorporates lignin, an insoluble
cross-linking compound.
 Wood and fibers are everywhere
Painting canvas
Clothing made from is made from
plant fibers flax or hemp
(cotton, linen) fibers.

Plant fibers are used for

making paper, and before
Wood is used for that papyrus.
buildings and
furniture.
 Ethanol ptoduced from cell wall cellulose is an important
energy source

Cell walls
from corn Ethanol
stalks and
other
agricultura
l residue

Image source: Genome Management Information System, Oak Ridge National Laboratory
THANK YOU
FOR YOUR
ATTENTION

My Biochemistry_project/2003