Midterm 3 Flashcards
What are membrane functions carried out by?
Membrane proteins
How much proteins make up animal membranes?
50% of the mass of most plasma membranes.
Glycolipids
Carbohydrates attached to lipids.
Glycoproteins
Proteins attached to lipids (short chains of sugars called oligosaccharides).
Why does the plasma membrane contain more lipid molecules?
Since they are much smaller, being over 50 more times prominent in the membrane.
Name a transporter protein and explain its function.
Na+ pump where it pumps Na+ out of the cell and K+ into.
Name an ion channel protein and explain its function.
K+ leak channel which allows K+ ions to leave the cell, having a great influence on cell excitability.
Name an anchor protein and explain its function.
Integrins which link intracellular actin filaments to extracellular matrix proteins.
Name a receptor protein and explain its function.
Platelet-derived growth factor (PDGF) receptor which binds extracellular PDGF, generating intracellular signals for the cell to grow and divide.
Name an enzyme protein and explain its function.
Adenylyl cyclase catalyzes the production of AMP in response to extracellular signals.
What are transmembrane proteins?
Proteins exist throughout the entire lipid bilayer, which part of their mass on each side (thus amphipathic).
How do the proteins on the cytosol side of the lipid bilayer associate with the membrane?
By an amphipathic alpha helix exposed on the surface of the protein.
How are the proteins that are entirely outside the bilayer, on either side, attached to the membrane?
Bound directly by one or more covalently attached lipid groups or indirectly through interactions with other membrane proteins.
How are integral membrane proteins removed from the bilayer?
By disrupting the bilayer with detergents.
How are peripheral membrane proteins removed from the membrane?
Gentle extraction procedures that interfere with protein-protein interactions but leave lipid bilayer intact.
How are the portions of a transmembrane protein connected?
By specialized membrane-spanning segments of the polypeptide chain.
What environment do these segments run through? What do they consist of?
Run through the hydrophobic environment of the interior of the lipid bilayer composed of amino acids of hydrophobic side chains (thus interact with the hydrophobic tails of the lipids).
What is the backbone of a polypeptide chain made of?
Protein amino acids, thus hydrophilic.
How do the atoms of the backbone interact with each other?
Can’t with interior of bilayer as no water, but hydrogen bond with one another.
How is hydrogen bonding maximized?
If the polypeptide chain forms a regular alpha helix.
How do the hydrophobic side chain and hydrophilic backbone exist in an alpha helix?
Hydrophobic side chain –> exposed on the outside of the helix to interact with hydrophobic lipid tails.
Hydrophilic backbone –> exist on the inside of the helix to form hydrogen bonds with one another.
What are single-pass transmembrane proteins? Give an example.
Its polypeptide chain only crosses the membrane once.
Ex. receptors for extracellular signals.
What are multipass transmembrane proteins? Give an example.
Those with series of alpha helices that cross the bilayer numerous times.
ex. channels
How are multipass transmembrane proteins arranged?
Amphipathic –> hydrophilic side chains fall one side of the helix and hydrophobic side chains on the others.
How is a transmembrane hydrophilic pore formed?
Multiple amphipathic alpha helices pack side by side to form a ring where the hydrophobic side chains are exposed to the lipids and the hydrophilic side chains form the lining of a hydrophilic pore.
How do transmembrane proteins cross the lipid bilayer as a beta sheet?
Amino acid side chains face the inside of the barrel to create a hydrophilic aqueous channel where the outside of the barrel is the hydrophobic core (interacts with the lipid bilayer).
What is a beta sheet?
A formation of a polypeptide chain that is rolled into a cylinder, forming a keg-like structure called a beta barrel.
What is an example of a beta barrel?
Porin proteins
What are porin proteins?
Form large, water-filled pores in mitochondrial and bacterial outer membranes.
What is the purpose of a porin protein?
Allow the passage of small nutrients, metabolites, and inorganic ions across the outer membranes.
What is the first step of separating membrane proteins?
Solubilizing the membrane with agents that destroy the lipid bilayer by disrupting hydrophobic associations.
What is the most widely used disruptive agent?
Detergents
How do detergents differ from membrane phospholipids?
Only a single hydrophobic tail.
What does the single hydrophobic tail of detergents allow?
One tail shapes it like a cone where they aggregate into small clusters in water forming micelles (spherical).
How do detergents disrupt the membrane?
The hydrophobic ends interact with hydrophobic regions of transmembrane proteins and tails of phospholipids, disrupting the lipid bilayer and separating the proteins from most of the phospholipids.
How does the detergent solubilize the membrane?
The hydrophilic ends interact, bringing the membrane proteins into solution as protein-detergent complexes that can be separated from one another.
How to determine a protein’s 3D structure?
X-ray crystallography
Why are membrane proteins harder to crystallize?
Purified in detergent micelles that are often heterogenous in size.
What is bacteriorhodopsin?
A small protein of 250 amino acids that are found in larger amounts of the plasma membrane of the Halobacterium halobium.
What does bacteriorhodopsin act as? Function?
A membrane transport protein (pump protein) that pumps H+ out of the cell.
How does bacteriorhodopsin gets its energy to pump H+ out of the cell?
Sunlight
What is the purpose of retinal in bacteriorhodopsin?
A light-absorbing non protein that gives the protein and bacteria a deep purple colour.
How is retinal attached to bacteriorhodopsin?
The hydrophobic molecule is covalently attached to one of bacteriorhodopsin’s seven transmembrane alpha helices.
What happens when retinal absorbs a photon of light?
It changes shape, causing the protein embedded in the lipid bilayer to undergo a series of small conformational changes.
What do the structural changes of bacteriorhodopsin result in?
The transfer of one H+ from the retinal to the outside of the bacterium.
How does the protein return to its original conformation (in terms of retinal)?
Retinal is regenerated by taking up a H+ from the cytosol, returning the protein to its original shape.
What is a pump protein?
A class of transmembrane proteins that actively move small organic molecules and inorganic ions into and out of cells.
How does bacteriorhodopsin create a concentration gradient?
When in the presence of sunlight, thousands of them pump H+ out of the cell generating a concentration gradient of H+ across the plasma membrane.
How are cell membranes strengthened and supported?
By a framework of proteins, attached to the membrane via transmembrane proteins.
What are plant’s plasma membrane encased by?
A cell wall
Explain the composition of a cell wall.
A meshwork of proteins, sugars, and other macromolecules.
What is the plasma membrane of an animal cell stabilized by?
Cell cortex.
What is the cell cortex made of?
A meshwork of fibrous proteins.
Where is the cell cortex attached?
On the underside of the plasma membrane (inside the cell).
What is the shape of red blood cells?
Biconcave shape
What is the main component of the cell cortex in red blood cells?
Dimeric protein spectrin
What is the structure of dimeric protein spectrin?
A long, flexible rod about 100nm in length.
How is the spectrin meshwork attached to the membrane?
Through intracellular attachment proteins the link it to specific transmembrane proteins.
What are the structures of anemic blood?
Red cells are spherical and fragile.
What are the main components of the cortex in animal cells?
Actin and motor protein myosin.
What is the purpose of the cortex?
Red blood cells need it to provide mechanical strength; need it to allow them to selectively take up materials from their environment; and cells use it to restrain the diffusion of proteins within the plasma membrane.
How was the lateral diffusion of proteins within the lipid bilayer shown?
Fusing a mouse cell with a human cell to form double-sized hybrid cell and then monitoring the distribution of certain mouse and human plasma membranes:
- confined to own halves of the newly formed cell
- time passes, and the two sets of proteins become evenly mixed over the entire cell surface
Membrane domains
Functionally specialized regions by confining particular proteins to localized areas within the bilayer membrane.
What can the plasma membrane tether itself to on the outside of the cell?
Membrane proteins attach to extracellular matrix or on an adjacent cell.
Can membrane domains interact?
Yes and no, as the cell can create barriers that restrict particular membrane components to one membrane domain.
Where must proteins that are involved in the uptake of nutrients from the gut located?
Apical surface (surface that faces the gut contents).
Where must proteins involved in the export of solutes out of epithelial cells into tissue and bloodstream located?
Basal and lateral surfaces.
What is the purpose of a tight junction?
Creates a seal between adjacent plasma membranes from specialized junction proteins forming a belt, thus not allowing membrane proteins to diffuse past it.
Proteoglycans
Membrane protein that contain one or more long polysaccharide chains.
Where are the carbohydrates attached to glycoproteins and glycolipids located? What do they form?
Located on the outside of the plasma membrane forming a sugar coating called glycocalyx.