ok, three questions: 1. Do we need to know about denaturing of proteins and the effects that has on structure? 2. What effect does being in an aqueous solution have on different bonds? 3. Do we need to know/what is the difference between saturated and unsaturated fats? Thank you for doing this!
I’m not the authority on this, as the test will be made by Dr. Spell, but it’s late and I will do what I can to set your mind at ease.
1. You should know as much as you need to explain what we did in class. We talked about how a pH change affects protein structure when we discussed hemoglobin’s oxygen binding affinity. Don’t worry too much about the mechanism, but be sure to brush up on interpreting graphs, equilibrium of reactions, etc.
2. I’m not sure what you mean by this. Are you talking about solubility? If so you should definitely be able to explain that.
3. We have not talked about this yet, so don’t worry. When we do it will be in the context of cell membranes and how their permeability is affected by “kinks” (double bonds) in the hydrocarbon chains.
Good answers. Here is what I would add:
1. To “denature” means to remove the inherent nature of something. The “nature” (i.e. structure) of proteins is determined by the kinds of interactions it has. Changes in pH can change the ability of the protein to hydrogen bond or ionic bond with itself (due to competition from all of those H+’s). Raising the temperature can cause those hydrogen bond sand van der Waals to fall apart. Changes in these interactions will change the shape; changes in shape can change the function. Hemoglobin was a good example of this.
2.Ionic bonds are very strong,except in water (due to competition from all those partial charges of the water).