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c) Lipid bilayer
d) Lipid bilayer plus protein lamellae e) Unit membrane f) Fluid-Mosaic model
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Membranes function properly only in the fluid state - T then fluidity; T then fluidity also The effects of fatty acid composition on membrane fluidity - depends on the length of fa present and degree of unsaturation of their side chains e.g. Membranes w/ Oleate (unsaturated fa) are more fluid than stearate (saturated fa)
The effects of sterols on membrane fluidity -cholesterol has the paradoxical effect of decreasing membrane fluidity at high T and increasing at low T (in animal CMs)
e.g. homeotherm or warm-blooded organismeffects on humans during chilly days, fingers get so cold that the membranes of sensory nerve endings cease to function, resulting in temporary numbness
and toes
How to regulate or compensate T changes? - by changing lipid composition of their membranes thru Homeoviscous adaptation ( in poikilotherms) -the main effect of this regulation is to keep the viscosity of the membrane approximately the same despite the changes in T Example: 1. Micrococcus (transferred from high T to low T results to an increase in the proportion of 16-C rather than 18-C fa in the PM thus minimizing effect of the low T.
*shorter fa chains decrease the melting T of a membrane 2. E. Coli (alteration in the extent of unsaturation of membrane fa rather than in length) -low T triggers synthesis of desaturase E that introduces double bonds into the HC chains of fa. - HVA also occurs in yeasts in plants (membrane fluidity depend on the increased solubility of oxygen in the cytoplasm at lower T) Oxygen- substrate of desaturase E Therefore: more Oxygen available at low T, more unsaturated fa synthesized at rapid rate and membrane fluidity increases Amphibians and reptiles adapt to lower T by increasing proportion of unsaturated fa in their membrane as well as cholesterol
Mammals or animals entering hibernation, the body T drops substantially but adapts to this change by incorporating a greater proportion of unsaturated fa into membrane phospholipids as its body T falls.
MEMBRANE PROTEINS -divided into 3 general classes:(based on the nature of their attachment
with the membrane)
embedded directly within the lipid bilayer(by the affinity of hydrophobic segments on the protein for the hydrophobic interior of the lipid bilayer)
inserted into the lipid bilayer but are associated with the membrane indirectly, generally by interactions with integral proteins(hydrophilic, located on the surface of the membrane where they are linked noncovalently to the polar head groups of phospholipids and/or to the hydrophilic parts of other membrane proteins)
a. Integral monotopic proteins - appear to be embedded on only one of the bilayer b. Singlepass proteins - transmembrane proteins that span the bilayer once c. Multipass proteins - span the bilayer multiple times - may consist of either a 1. single polypeptides 2. several associated polypeptides (Multisubunit proteins)
d. Peripheral membrane proteins - too hydrophilic to penetrate into the membrane - attached to the membrane by electrostatic and H-bonds that link them to adjacent membranes proteins or to phospholipid headgroups
Lipid-anchored membrane proteins -covalently bound to lipid molecules that are embedded in the lipid bilayer 1. Fatty-acid or prenyl group proteins on the inner surface of the membrane 2. Glycosylphosphatidylinositol (GPI) -most common lipid anchor -proteins on the outer membrane surface
Aquaporin
2 Categories of Transport
1. Non- carrier mediated does not require carrier proteins(simple diffusion) 2. Carrier-mediated requires specific carrier proteins a. facilitated diffusion (uniport) b. active transport
2. Polarity: bilayer CH3-CH2-CH2-OH more permeable (Propanol) to nonpolar molecules 3. Ionic: bilayer highly impermeable to ions O2 (oxygen)
109:1
*Ratio of diffusion rate for the permeable solute to the less permeable solute
Channel proteins
-facilitate diffusion by forming hydrophilic trans-membrane channels
3 Kinds: 1. Ion channels - transmembrane proteins that allow rapid
passage of specific ions (remarkably selective) - single channel can conduct almost a million ions per second! -most ion channels are gated (opened and closed by conformational changes in the protein regulating the flow of ions thru the channel)
3 gated channels:
1. Voltage-gated = open and close in response to changes in membrane potential 2. Ligand-gated = triggered by the binding of specific substances to the channel protein 3. Mechanosensitive = respond to mechanical forces that act on membrane
2. Porins
- transmembrane proteins that allow rapid passage of various solutes -pores found in the outer membranes of mitochondria, chloroplasts and bacteria -larger & much less specific -formed by multipass transmembrane proteins -made of closed cylindrical sheet called barrel -inside pore (water-filled) is lined by polar chains while outside that of nonpolar side chains -pore allows passage of various hydrophilic solutes with size depending on the pore size of the particular porin
3. Aquaporins (AQPs)
-transmembrane that allow rapid passage of water
Active Transport
-ATP-powered pumps that transport ions and various small molecules against their concn gradient
2 types: -based on the energy source 1. Direct active transport -also called primary active transport -accumulation of solute molecules or ions on one side of the membrane coupled directly to an exergonic reaction particularly hydrolysis of ATP. -transport proteins driven directly by ATP hydrolysis are called ATPases or ATPase pumps.
2. Indirect active transport -also called secondary active transport -depends on the cotransport of two solutes with the movement of 1 solute down its gradient driving the movement of the other solute up its gradient.
-transport ATPases or pumps are responsible for most direct active transport in both prokaryotic and eukaryotic cells.
Figure 15-10. The four classes of ATP-powered transport proteins. P-class pumps are
composed of two different polypeptides, and , and become phosphorylated as part of the transport cycle. The sequence around the phosphorylated residue, located in the larger subunits, is homologous among different pumps. F-class and V-class pumps do not form phosphoprotein intermediates. Their structures are similar and contain similar proteins, but none of their subunits are related to those of P-class pumps. All members of the large ABC superfamily of proteins contain four core domains: two transmembrane (T) domains and two cytosolic ATP-binding (A) domains that couple ATP hydrolysis to solute movement. These core domains are present as separate subunits in some ABC proteins (depicted here), but are fused into a single polypeptide in other ABC proteins.
Kind of Membrane
Kind of Organisms
Function of ATPase
H+
Plasma membrane
Plants, fungi
Ca2+
Plasma membrane
Eukaryotes
V-type ATPases (V for vesicle H+ Lysosomes;secretory vesicles Vacuolar membrane Animals Keep pH in organelle low, which activates hydrolytic enzymes Keeps pH in vacuole low,which activates E
H+
Plants, fungi