What statement about "peripheral" membrane proteins is INCORRECT?   Hide answer choices  Polar interactions of peripheral protein and polar head groups of the membrane lipids can be disrupted by adding salts or by changing the pH.   They are membrane proteins that are anchored to the membrane by a covalently attached lipid molecule.   They are membrane proteins that interact with the polar head groups of the membrane lipids.   They are membrane proteins that bind to the surfaces of integral proteins.   They are membrane proteins that traverse the lipid bilayer.

Human Physiology: From Cells to Systems (MindTap Course List)
9th Edition
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Lauralee Sherwood
Chapter3: The Plasma Membrane And Membrane Potential
Section: Chapter Questions
Problem 5RE: Using the answer code on the right, indicate which membrane component is responsible for the...
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  1. What statement about "peripheral" membrane proteins is INCORRECT?

     
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    1. Polar interactions of peripheral protein and polar head groups of the membrane lipids can be disrupted by adding salts or by changing the pH.

       
    2. They are membrane proteins that are anchored to the membrane by a covalently attached lipid molecule.

       
    3. They are membrane proteins that interact with the polar head groups of the membrane lipids.

       
    4. They are membrane proteins that bind to the surfaces of integral proteins.

       
    5. They are membrane proteins that traverse the lipid bilayer.

       
     

    2. What is the difference between the T form and R form of the hemoglobin molecule?

     
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    1. The T form of the hemoglobin molecule is not constrained by subunit–subunit interactions.

       
    2. The T form of the hemoglobin molecule is unstable without 2,3-BPG.

       
    3. The R form of the hemoglobin molecule has the oxygen-binding sites free of strain.

       
    4. The R form of the hemoglobin molecule has a pocket in the center of the tetramer for 2,3-BPG.

       
    5. The R form of the hemoglobin molecule is unstable

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