BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Chapter 13, Problem 32P
Interpretation Introduction
Interpretation:
Three protein classes involved in ion transport on the basis of their different characteristics should be compared
Concept introduction:
The membrane permeability is achieved with the help of various classes of proteins such as pumps, carriers, and channels. Each of the three classes have a specific role to play.
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What would happen in each of the following cases where something related to intracellular transport is altered? Assume in each case that the protein involved is a soluble protein, not a membrane protein. State where each protein would be located and explain each of your answers.
You add a signal sequence (for the Golgi) to the N-terminal end of a normally cytosolic protein.
You change the hydrophobic amino acids in an ER signal sequence into other, hydrophobic, amino acids.
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?
Chapter 13 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
Ch. 13 - Prob. 1PCh. 13 - Prob. 2PCh. 13 - Prob. 3PCh. 13 - Prob. 4PCh. 13 - Prob. 5PCh. 13 - Prob. 6PCh. 13 - Prob. 7PCh. 13 - Prob. 8PCh. 13 - Prob. 9PCh. 13 - Prob. 10P
Ch. 13 - Prob. 11PCh. 13 - Prob. 12PCh. 13 - Prob. 13PCh. 13 - Prob. 14PCh. 13 - Prob. 15PCh. 13 - Prob. 16PCh. 13 - Prob. 17PCh. 13 - Prob. 18PCh. 13 - Prob. 19PCh. 13 - Prob. 20PCh. 13 - Prob. 21PCh. 13 - Prob. 22PCh. 13 - Prob. 23PCh. 13 - Prob. 24PCh. 13 - Prob. 25PCh. 13 - Prob. 26PCh. 13 - Prob. 27PCh. 13 - Prob. 28PCh. 13 - Prob. 29PCh. 13 - Prob. 30PCh. 13 - Prob. 31PCh. 13 - Prob. 32P
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- 1) You are studying a transport protein. It appears to bind temporarily to the molecule to be transported. During normal transport, no energy is expended. The addition of a particular molecule that closely resembles the normally transported molecule inhibits transport. An increase in the concentration of the normally transported molecule in the presence of a constant concentration of the inhibitor increases the rate of transport. What kind of transport is described? 2) What are peripheral membrane proteins?arrow_forwardName the three groups into which membrane-associated proteins may be classified. Explain the mechanism by which each group associates with a biomembrane.arrow_forwardWhat would happen in each of the following cases where something related to intracellular transport is altered? Assume in each case that the protein involved is a soluble protein, not a membrane protein. State where each protein would be located and explain each of your answers. You change the hydrophobic amino acids in an ER signal sequence into negatively charged amino acids. You discover a protein that has both an ER signal sequence and a nuclear localization sequence. The ER signal sequence is at the N-terminus of the protein, and the nuclear localization sequence is located in the middle of the protein.arrow_forward
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