In the first section of this page, you will write a daily summary of that day's class.  For example in  your chapter 2 blog, your first entry should be titled 9/3/10.  You should then write a one or two paragraph summary of that day's lecture, outlining the major points.  In the second section, you are required to add two items (link to a website, video, animation, student-created slide show, student-created PowerPoint presentation) and one journal article pertaining to a topic in this chapter.  A one-paragraph summary must accompany each item describing the main idea and how it applies to the lecture topic.  Please see the PBWorks help guide for assistance embedding video and other items directly in the page.  I will also produce a how-to video on using tables to wrap text around items and other useful tips.  Please see the syllabus for organization and grading details.

A.  Daily Blog

October 13, 2010: I am pretty sure that Dr. Weber looked at MOST(not mike) of the guys as if we were crazy or we take days like "International Suit-Up Day" way to seriously. However, personally I enjoyed suiting up and looking all professional. Anyway, we began the our discussion with what was energy. What I understood from this was that energy is the force that makes us do work (I automatically pictured the Nike logo as well as the swoosh sign  and made a weird but helpful connection). There are many forms of energy that surrounds us, but we specifically looked at kinetic and potential energy. Kinetic energy is associated with the movement that goes on with an object. Potential energy was connected to the position and structure of the object. These terms can easily be memorized, but what really made sense was when I looked back into the previous chapters that we covered. For example, as soon as I heard the word: potential, concentration gradients and how potential energy was formed when ions went from a low to high concentration. It was coming back to me and made a lot of sense! Along with gradients re-appearing, the laws of Thermodynamics was briefly discussed in today's lectures. A lot of connections to how energy is transferred and how there is an increase entropy were made in class which helped in understanding how energy "worked". 

     One thing that I found really interesting was how Dr. Weber told us that as human beings, we contradict the 2nd law of thermodynamics. The first thing that popped in my head was HOW? Then he explained how the 2nd law states that there is an increase in entropy which is basically the breaking down of highly organized objects to unorganized objects. "If this was true for humans, we just be a bunch of atoms floating around" is what Dr. Weber said and made complete sense! The reason we have highly organized things in our body is so that they can carry out complex functions. We also discussed where potential energy can be found and where energy is required to move certain things. I use the idea of a slide to picture how energy is released and energy is used to create movement. When you move down the slide, you are very unstable and therefore have a lot of potential energy. When you are at the bottom and want to climb to the top, you need an input of energy in order to get that driving force to reach your destination. In reality this actually makes SOO much sense. Next time you go to the park, go down a slide and then try climbing to the top. It is tougher than it seems. Towards the end of class we talked about the necessary amount of energy inputed in oder to balance out the energy being released. We looked at an example: Fructose ------> Fructose-1,6-bisphosphate. Using the information we learned from ATP hydrolysis, we had to determine how much of each substance was required in order for this reaction to occur. It felt like chemistry! 

October 15, 2010: Today, we started to talk about the role of enzymes! We have had a small introduction to enzymes previously since we did a lab on it earlier. So what Dr. Weber stressed on in class was that enzymes are not energy makers for reactions. They merely lower the activation energy and speed up the reaction. I mean we could always add heat to carry out the reaction, but then certain factors have to be added in when dealing with heat such as: what is the cell's optimal temperature in our body? what could possibly happen to the proteins? (everything always comes back to proteins doesn't it?). The optimal temperature for a body cell is about 37 degree's Celsius. If we were to increase the heat past this level, it could create a hazardous working environment. Along with this the PROTEINS WOULD DENATURE!!! We definitely don't want that happening, So that's where enzymes come in! They steer away from the usage of heat and instead bring the molecules closer together in order for their bonds to rearrange into the product needed for the cell. Enzymes are proteins which means they have a weird and globular structure. They have two main features (but have many more smaller ones) which are their active sties and the substrates for the enzyme. The active site is where the reaction takes place. I think of it as where the action takes place in the enzyme. As for the substrate, it is the molecule that is being attached to the enzyme at the active site. We then started to talk about the amount of substrate required compared to the enzyme activity. This was then used to determine what was a V-Max and Km. V-Max is the velocity of reaction near the maximal rate. This is basically where the graph plateau's because all the enzymes present are filled up with substrates. 

     We then discussed about different inhibitors. The ones that we discussed are Competitive and Non-Competitive. Competitive inhibitors are like "guard substrates".  They are structurally similar to the substrate being broken down and can fit in the active site. This prevents the substrate from binding to the active site and producing more products. Another way to prevent the enzyme from forming products is by Non-Competitive Inhibition. This is when a molecule binds to the allosteric site of the enzyme to change the shape of the enzyme. This way the substrate can't bind to the active site. We then looked at different graphs that represented Competitive and Non-Competitive Inhibition. We noticed that in Competitive Inhibition, more substrate is required, but the graph ended reaching its V-Max. However, in the Non-Competitive Inhibition no matter how much substrate was added, the enzyme would never reach its V-Max. I am still questioning why that occur, but maybe I can find an article on that which can help me out!

B.  Useful Materials