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.

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.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter32: The Reception And Transmission Of Extracellular Information

Section: Chapter Questions

Problem 11P

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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 glycoprotein
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 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
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 BOTH
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?)
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 BOTH
Three mechanisms by which membrane-bind-ing proteins bend a membrane are illustrated in FigureQ10–2A, B, and C. As shown, each of these cytosolic mem-brane-bending proteins would induce an invagination ofthe plasma membrane. Could similar kinds of cytosolicproteins induce a protrusion of the plasma membrane(Figure Q10–2D)? Which ones? Explain how they mightwork.
3- Which is incorrect regarding ligand-protein binding reactions?a. Allosteric modulation of the protein’s binding site occurs directly at the binding site itself.b. Allosteric modulation can alter the affinity of the protein for the ligand.c. Phosphorylation of the protein is an example of covalent modulation.d. If two ligands can bind to the binding site of the protein, competition for binding will occur.e. Binding reactions are either electrical or hydrophobic in nature.
What is the likely identity of these membrane associated proteins: (a) a protein that is released from a membrane treated with a high salt solution, which causes disruption of ionic linkages; (b) a protein that is not released from the membrane upon its exposure to a high salt solution alone, but is released when the membrane is incubated with an enzyme that cleaves phosphate glycerol bonds and covalent linkages are disrupted; (c) a protein that is not released from the membrane upon exposure to a high salt solution, but is released after the addition of the detergent sodium dodecylsulfate (SDS). Will the activity of the protein released in part (c) be preserved following its release?
You are interested in the mobility of two different unknown integral plasma membrane proteins—protein X and protein Y—in a cell. In one cell, you fluorescently label all the X proteins. In another cell, you label all the Y proteins. When you perform FRAP analysis on both cells, you find that most of the protein X fluorescence has recovered within 3 minutes, but recovery of the protein Y fluorescence is significantly slower. Even after 10 minutes, only 50% of the protein Y fluorescence has recovered. Describe the FRAP experimental protocol, explain what the results tell you about mobility of the X and Y proteins, and propose a possible explanation for why the mobilities of the two proteins differ.
1. Why is it important that membrane lipids have dual character-part of the molecule is hydrophilic and part of the molecule is hydrophobic? 2. Why do you suppose lecithin are often added to processed foods such as hot Choco mix? 3. List down the common glycerophospholipids in membrane? 4.What is the predominant sphingolipid in myelin sheath? Why? 5. Name the structural unit for a molecule to be classified as a a. Phospholipid b. Glycolipid c. Sphingolipid 6. Explain emulsification in mayonnaise.
*answer only C Figure 1 represents the amino acid sequence of a G-protein coupled receptor (GPCR) as determine by mass spectrometry. *Figure 1 is shown as in the added image. Figure 1: The amino acid sequence of a GPCR as determined by mass spectrometry.(a) Describe the general structural features of this GPCR. (b) A ligand called TIIF binds to arginine-127 (R127 in transmembrane helix 3(TMH3) to cause the activation of this GPCR. There are more than one arginine residues in this GPCR, why was the 127R selected by the ligand? (c) Describe a spectroscopic technique that you can use to determine the structure of the GPCR apart from mass spectrometry.
Which factor has NOT been shown to play a role in determining the specificity of protein kinases? a. protein tertiary structure b. protein quaternary structure c. primary sequence at phosphorylation site d. disulfide bonds near the phosphorylation site e. residues near the phosphorylation site