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So does the actual conformational change ITSELF require energy? I'm assuming that the overall effect of facilitated diffusion is an increase in entropy by "spreading out" the solute as much as possible, but at times doesn't the solute move from an area of lower concentration to an area of higher concentration, just not at as fast as the rate of solute moving from a higher concentration to a lower concentration? I guess I'm kind of thinking about it like a chemical reaction, where reactants are being converted to products and products to reactants, but not necessarily at the same rate. So when the protein undergoes a conformational change, is this isolated process favorable?
Last edited by MedHopeful114; 06-11-2012 at 07:18 PM. |
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The conformational change that occurs when the ligand binds to the membrane transporter protein is "powered" by the protein simply seeking its most thermodynamically stable orientation. Given the various factors within the cell, the transport protein's affinity for the ligand could be quite high on the side of the membrane with the larger concentration of the ligand. This would make it more favorable to bind to the ligand. One this binding takes place, however, the membrane transporter protein could alter its physical structure due to induced-fit binding or just a conformational change. Now, the protein may no longer have the same affinity for the ligand. Another consequence of this conformational change is that the transporter protein now may be able to achieve its most thermodynamically stable state by releasing the ligand on the other side of the membrane. This long and enduring explanation just restates how natural processes seek out their most stable thermodynamic state and, as they seek this state, free energy may become available. |
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