1 SEM CARDLESS ACC W/RAVEN TEXT
1 SEM CARDLESS ACC W/RAVEN TEXT
12th Edition
ISBN: 9781265321062
Author: Raven
Publisher: MCGRAW-HILL HIGHER EDUCATION
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Chapter 5, Problem 3S

The distribution of lipids in the ER membrane is symmetric, that is, it is the same in both leaflets of the membrane. The Golgi apparatus and plasma membrane do not have symmetric distribution of membrane lipids. What kinds of processes could achieve this outcome?

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A transmembrane protein has the following properties: it has two binding sites, one for solute A and one for solute b. The protein can undergo a conformational change to switch between two states: either both binding sites are exposed exclusively on one side of the membrane or both binding sites are exposed exclusively on the other side of the membrane. The protein can switch between the two conformational states only if both binding sites are occupied or if both binding sites are empty, but cannot switch if only one binding site is occupied. What kind of protein do these properties define?
A transmembrane protein has the following properties: it has two binding sites, one for solute A and one for solute b. The protein can undergo a conformational change to switch between two states: either both binding sites are exposed exclusively on one side of the membrane or both binding sites are exposed exclusively on the other side of the membrane. The protein can switch between the two conformational states only if both binding sites are occupied or if both binding sites are empty, but cannot switch if only one binding site is occupied. Do you need to specify any additional properties to turn this protein into a symport that couples the movement of solute A up its concentration gradient to the movement of solute b down its electrochemical gradient?
Proteins may be bound to the exoplasmic or cytosolic face of the plasma membrane by way of covalently attached lip- ids. What are the three types of lipid anchors responsible for tethering proteins to the plasma membrane bilayer? Which type is used by cell surface proteins that face the external medium? By glycosylated proteoglycans?
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