3. When you think about the primary structure of the mannose-6-P receptor, assuming that it is an integral membrane protein with one membrane-spanning domain and assuming that it has a ERSS, what are all of the different protein domains that must be present in this protein's primary structure to get it to where it needs to go and to carry out all of the functions/activities? (Draw a schematic of the protein structure/sequence and explain each region).
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- 1a-Membrane bound proteins often contain transmembrane domains. These transmembrane domains contain higher amounts of which of the following. Select all that apply. Select one or more: a. Non polar amino acids b. Polar amino acids c.Polar charged amino acids d. Amino acids with hydrophillic residues (R groups) 1b-In most cases, the major function of protein kinases is to: Select one: Oa.Add phosphate groups to certain proteins O b. Hydrolyze GTP to GDP O c. Add CAMP to adenylyl cyclase O d. Facilitate binding of signalling molecules to the associated membrane bound receptor.1. What cellular event happens in response to the binding of a growth factor to its respective receptor on the membrane of the growth factor’s target cell? Describe what happens to a tyrosine kinase receptor once it binds the growth factor signal. 2. Describe the three domains of a receptor tyrosine kinase. Explain the structure of the transmembrane domain and the amino acid composition and arrangement of this part of the receptor PLEASE ANSWER BOTH2. Describe the three domains of a receptor tyrosine kinase. Explain the structure of the transmembrane domain and the amino acid composition and arrangement of this part of the receptor
- 3. How does dimerization of a receptor tyrosine kinase promotes autophosphorylation of the intracellular domain of the receptor? How does the formation of a dimer helps the phosphorylation reaction?4. Describe where is the phosphate group added on a protein when it gets phosphorylated (what amino acid? what atom?). Then list all the ways that protein function may change after it gets phosphorylated PLEASE ANSWER BOTHDiscuss Concepts Describe the possible ways in which a G-proteincoupled receptor pathway could become defective and not trigger any cellular responses.1. List one example of AMPLIFICATION OF SIGNAL during the cell’s response to Hedgehog. Makesure to write out full steps and not just the name of a protein. Do not choose the example from2h or 2i if you chose amplification of signal as your answer to those questions.
- 6. Define a receptor tyrosine kinase and distinguish it from a serine/threonine kinase. (As we discuss ANY kinase in signalling pathways, pay close attention to what type of kinase it is...does it phosphorylate serene/threonine resides or tyrosine residues?). which of the following statements about heterotrimetric G proteins and their receptors is incorrect? A: when GTP binds to the alpha subunit of the G protein, the beta-gamma subunit dissociates from the alpha subunit B: G-protein coupled receptors contain nine transmembrane alpha helices C: binding of arrestin causes removal of the receptor from the membrane D: G protein- coupled receptors may be desensitized by serine phosphorylation I had chosen option A and got it wrong. What is the Correct answer and explain how it is. Also, where did i go wrong in choosing option A?The voltage-gated calcium channel is a protein that is imbedded and spans the lipid membrane to allow the movement of calcium into the axon terminal. What is theappropriate amino acid configuration of this channel that allows this movement to happen?Select one:O a. non-polar amino acids on the interior surface and polar on the exterior surfaceO b. polar amino acids on the interior surface and polar on the exterior surfaceO c. non-polar amino acids on the exterior surface and polar on the interior surfaceO d. non-polar amino acids on the interior surface and non-polar on the exterior surface
- Two proteins have exactly the same amino acid sequence. Protein A is able to bind with high affinity to a cellular receptor, while Protein B cannot bind to the receptor under identical conditions. In 3-4 sentences explain, provide an explanation why two proteins with the same primary sequence could have very different abilities to bind a receptor.Sequence analysis of a membrane protein shows four 20-amino acid long stretches of residues that are predominantly hydrophobic. Between each of these stretches of hydrodophobic residues, a stretch of predominantly hydrophilic residues is found. From this observation one can reasonably postulate that: A. this is a peripheral membrane protein which interacts with the membrane via hydrophobic interactions B. this protein has 4 alpha helical segments that span the membrane C. this protein can be removed from the membrane by dramatically increasing the salt concentration. D. this is a 4 stranded beta barrel which spans the membrane E. this is a glycoproteinSequence analysis of a membrane protein shows four 20-amino acid long stretches of residues that are predominantly hydrophobic. Between each of these stretches of hydrodophobic residues, a stretch of predominantly hydrophilic residues is found. From this observation one can reasonably postulate that: A. this is a peripheral membrane protein which interacts with the membrane via hydrophobic interactions B. this protein has 4 alpha helical segments that span the membrane C. this protein can be removed from the membrane by dramatically increasing the salt concentration. D. this is a 4 stranded beta barrel which spans the membrane E. this is a glycoprotein Facilitated diffusion (passive transport) through a biological membrane is A. driven by a concentration gradient. B. generally irreversible. C. endergonic. D. driven by the ATP to ADP conversion