How do single pass and multi-pass transmembrane proteins become inserted into a membrane?
Which is true of Receptor Tyrosine kinases? Most RTK subunits are single-pass transmembrane proteins. They are seven-pass transmembrane proteins. They are coupled to ion channels in the membrane They contain lots of tyrosine residues in their transmembrane domains
#3 2. Explain the synthesis of lipids at the ER membrane and how transmembrane proteins are inserted. 3. Compare and contrast types of membrane transport including transport proteins.
27. Integrins are single-pass integral membrane proteins in the plasma membrane of animal cells and are involved in the interaction of the cell with the surrounding extracellular matrix. Which of the following descriptions do you think matches the transmembrane part of an integrin molecule? A. It forms a B barrel. B. It is an a helix that is bent in the middle. C. It is about 10 amino acids long, with every other amino acid side chain being hydrophobic. D....
What is Co-translational insertion of secreted and transmembrane proteins into the ER membrane including translocon, secreted proteins, type 1 transmembrane protein, type 2 transmembrane proteins?
Match the following: Integral (intrinsic) membrane proteins Transmembrane protein Porins C-- Lipid-linked proteins Peripheral (extrinsic) proteins 1. Channel-forming proteins found in the outer membranes of bacteria, with a beta-barrel motif. 2. Proteins that are associated with membranes, but can be dissociated by relatively mild procedures. 3. Proteins that completely span the membrane. 4. A general class of proteins that are tightly bound to membranes by hydrophobic interactions. 5. Membrane-associated proteins that have covalently-bonded lipids.
What do all β-barrel transmembrane proteins have in common? A. The number of β strands. B. The diameter of the barrel. C. The number of negative peaks in their hydropathy plots. D. The general function, i.e. membrane transport. E. The structural rigidity compared to α-helical transmembrane proteins.
Is every isotonic solution isosmotic? Explain and provide an example. Many membrane proteins contain transmembrane segments (ie segments which penetrate through the membrane). How must these proteins be formed to allow them to act as an ionic channel? What specialisation would you need to allow it to function as a voltage-gated channel? If sodium is a smaller ion than potassium, then how can a channel be specific for potassium (ie. does not also allow sodium through)?
What problem do transmembrane proteins encounter in spanning the bilayer? Describe a structure by which transmembrane proteins overcome this problem
1. Explain how the amphipathic nature of membrane proteins helps form the three-dimensional structure of a single-pass protein like a receptor, versus a multipass protein like a channel. 2. Describe the different ways by which cells confine proteins or restrict protein movement to a specific region of the plasma membrane
Determine whether the following classes of proteins are synthesized on free ribosomes or ER docked ribosomes. a) Single-pass membrane proteins b) Multi-pass membrane proteins c) Peripheral membrane proteins (on the cytosolic side) d) Peripheral membrane proteins (on the luminal side) e) Peripheral membrane proteins (on the extracellular side) f) Fatty acid-anchored membrane proteins g) GPI- anchored membrane proteins - Where would a protein likely go if you were to remove a characteristic hydrophobic membrane spanning domain?