3. Here is a question that test your ability to understand and combine concepts.hydropathy indexI.II.III.IV.V.50100amino acid numberShown on the left is a hydropathy plot of a plasmamembrane integral protein lacking beta strandstructures. It contains three domains A, B and C.Would you predict this protein to containtransmembrane helices? If so how many?If this protein is a Type-ll membrane protein, whichregion do you expect to be exposed to aqueousenvironment of the extracellular side (choose from A, Band C)? Why?Where do you expect to see positive charged residues?You can mention the rough residue numbers or useregion, A, B or C to help convey your message. Explainyour reasoning.Where do you expect to see aromatic residues? Explainyour reasoning.

I. Would you predict this protein to contain transmembrane helices? If so, how many? Hydropathy plot…

Answered: 3. Here is a question that test your…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Many transmembrane proteins are oligomeric, with several identical subunits. The oligonmers are usually found to have some form of C, symmetry, rather than D, or any higher order. Suggest a reason for this observation.
The following hydropathy plot was obtained for an unknown membrane protein. -2. 20 40 60 Residue number It is also known that that this protein cannot be extracted from the membrane using concentrated salt solution or change in pH. What kind of membrane protein is this? Integral membrane protein that crosses membrane mnulople.times. Lipid-Iinked membrane proten. Peripheral membrane protein. Hydropathy index 2.
Distinguish between transmembrane proteins, integral proteins, and peripheral proteins. 7. Integral proteins are often found spanning the membrane of a cell or organelle. These proteins serve as channels for specific molecules to travel through the membrane, either into or out of the cell. Indicate on the picture of the integral protein where you would most likely find amino acids with hydrophobic R-groups. Next, indicate on the picture of the integral protein where you would most likely find amino acids with hydrophilic R-groups. Explain your reasoning.
The transmembrane segments of most integral membrane proteins are made of alpha -helical secondary structures. What is the advantage of this conformation ? How do multiple alpha-helices arrange themselves to form the aqueous pore of an ion channel ?
We discussed four types of lipid movements in the membrane (rotational, diffusion, flexion, flip- flop). Choose TWO of the four and 1. describe the movement of molecules through the channel or transporter, and 2. explain why it creates motion (membrane fluidity) in a plasma membrane.
What are the key differences between rough endoplasmic reticulum and smooth endoplasmic reticulum. It would be very helpful if its in tabular form. Please help me. Thank you
Your research advisor would like you to measure the movement of a protein X using FRAP. The results of your FRAP experiment are shown below. What can you conclude? Fluorescence Intensity (Arbitrary Units) Time (Seconds) Time point of exposure to an intense laser Protein X appears to be completely immobilized in the membrane Protein X appears to be partially immobilized in the membrane You cannot make predictions about the mobility of Protein X with these data Protein X appears to be completely mobile in the membrane
What typical structure[s] is/are found in integral membrane proteins – how do they span themembrane?
+H₂N-CH-COO™ 1 CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. amino acid D O amino acid B amino acid C O amino acid A +H₂N-CH-COO™ 1 amino acid E C=O B. Of the four amino acids shown, this amino acid would most likely be located in the transmembrane domain of an integral membrane protein. +H₂N-CH-COO™ 1 CH₂ 1 OH C. +H₂N-CH-COO™ I CH H₂C CH₂ D.
Choose from the dropdown menu, the description that best matches each of the components shown. A se C D. [ Select ] A: multipass transmembrane protein phospholipid polar heads single pass transmembrane protein B: peripheral membrane protein lipid-anchored protein C: ( Select ] D: [ Select ] E: [ Select ] MacBook Air B
6. Sort the following molecules based on their rate of diffusion across the phospholipid bilayer in the absence of any transporter, from highest (1) to lowest (4). Glucose 0₂ H₂O Protein kinase A
Drawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (a) From the list below, select the amino acid(s) that might by more common in the extracellular domain of this membrane protein and whose side- chain can form hydrogen bonds with the surrounding water molecules. Explain why you selected this option(s). Lysine Serine Phenylalanine Methionine (b) From the list below, select the amino acid(s) that would likely be found in the transmembrane/ membrane spanning domain of this protein and whose side- chain interacts with the lipid bilayer. Lysine Serine Phenylalanine Methionine

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