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differences in membrane composition differentiates organelles by
dictating shape, curvature, function
examples of membrane composition differentiating organelles
mitochondria (cardiolipin rich —> supports the ETC)
ER: phosphaticlycholine- rich (flexible synthesis site)
Plasma membrane= cholesterol and sphingolipids (rigidity and signaling)
rafts
regions of the membrane that are less fluid, holding proteins together for localized interactions
what makes up rafts
cholesterol and glycosphinolipids
cholesterol helps rafts by
modulating fluidity and permeability (decreasing) and thickening the eukaryotic membrane and causes an increase order
lipid distribution in a leaflet
not random or even
why is lipid distribution in a leaflet not random nor even
dictated by things like cholesterol and different interactions like the hydrophobic effect and it isn’t even because it is asymmetric
glycosphingolipids
increase rigidity by having longer chain tails
job of rafts (proteins)
rafts allow for separation of proteins in the membrane
functions of biological membranes
define boundaries of the organism or cell
allow for selective import/export AKA selective permeability
maintain metabolites and ions within the cell
sense external signals and transmit information into the cell
provide compartmentalization within the cell
produce and transport nerve signals
store energy as a proton gradient and support synthesis of ATP
how does selective permeability work
import of nutrient (e.g. lactose)
export of waste and toxin (e.g. antibiotics)
provide compartmentalization within the cell
separate energy= producing rxns from energy consuming rxns
keep proteolytic enzymes away from important cellular proteins
membrane fusion
special property of the fluid mosaic model which states that membranes can fuse separately without losing continuity (no loss of contents)
fusion preserves the hydrophobic barrier while mixing membranes
vesicles can also be removed from the surface membrane
spontaneous fusion
can occur between lipid bilayers under favorable conditions
protein mediated diffusion
required for specific events- viral entry into host cell, neurotransmitter release, and vesicle trafficking
double membranes
can create an inner-membrane space useful for gatekeeping or energy storage
examples, mitochondria and E.coli inner membrane
mitochondria double membrane
serves as an energy reservoir—> proton gradient
Ecoli double membrane
outer membrane- often contains porin (beta barrel proteins) for diffusion
inner membrane- highly selective, houses energy conservation enzymes
chemical potential
depends on the concentration difference
electrical potential
depends on charge imbalance
electrochemical potential
combined force of an electrical difference and a chemical concentration difference across a membrane, which influences the movement of charged ions.
integral membrane proteins
span the bilayer—> facilating some kind of support
membrane proteins are either all helical or all beta sheet within the membrane
alpha helical proteins
dominate eukaryotic membranes (transports, receptors)
beta barrel proteins
found in bacterial outer membranes
helical
transport, signaling, and energy production
Trp and tyr in integral proteins
stabilize protein at the hydrophilic and hydrophobic interface because of their amphipathic side chains.
porins
beta sheet structures with a hole in the middle that allows small molecules to pass through
general functions of integral membrane proteins
solute transport, signal transduction, cell adhesion, and energy conversion
membrane protein insertion
membranes integrated into a membrane must be added to the membrane during translation
how do membrane proteins insert themselves onto the membrane
insert co translationally during synthesis on ribosomes bound to the rough ER
Sec 61
translocon acts as a protein- conducting channel, integrating hydrophobic transmembrane domains into the lipid bilayer.
transport for catalysis
integral membrane proteins catalyze diffusion of molecules across the membrane
polar molecules and ions don’t move spontaneously across the membrane because
unfavorable to desolvate or dehydrate them
how do transporters reduce the activation energy
provide polar binding sites that shield ions from the hydrophobic core
membrane proteins accelerate ion transport by how much
10^12 s^-1
simple diffusion
small nonpolar molecules down the concentration gradient
facilitated diffusion
down the the electrochemical gradient
large nonpolar molecules= glucose
amino acids
ions
primary active transport
uses ATP hydrolysis against the electrochemical gradient
Na+/K+ ATPase
SERCA
secondary active transport
against electrochemical gradient driven ion moving against gradient
lac permease
Na+/glucose transporter
channel proteins
show fast diffusion because of continuous pores
carrier proteins/transport proteins
slow diffusion because a conformational change must happen when a ligand binds to the protein and behave like Michaels- Menten like saturation
glucose uptake in intestinal cells
Na+glucose symport into cell (secondary active)
GLUT2-mediated exit (uniport) (facilitated diffusion)
Na+/K+ ATPase resets Na+ gradient (primary active)
glucose transporter structure
GLUT proteins contain 12 alpha helicies forming a central cavity for glucose to bind to
the rocker switch mechanism alternates between outward-open- and inward open states exposing the binding site one side at a time
Trp and Tyr at interface stabilize helix orientation and anchor the transporter in the membrane.