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Chapter 3 Blog:  The Chemical Basis of Life II (Kimberly)

Page history last edited by Kimberly Balao 13 years, 10 months ago

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

 

9/10/10: Today in lecture we covered chapter sections 3.1, 3.2 and 3.4 We learned a bit about organic chemistry. We learned that organic chemistry deals with all the molecules that contain carbon. Carbon has four valence electrons, so it can make a variety of different bonds. We learned about isomers, which are two molecules with the same molecular formula but different structural formula. In this chapter we learned that the properties of molecules really depend on the structure and not the chemical composition. Different type of isomers are structural isomers and enantiomers. Enantiomers are like two molecules that are mirror images of each other. Lastly we went into details of the many functional groups. Functional groups are groups of atoms with the same chemical properties in all the molecules in which it occurs. 

 

9/15/10: Today we talked about in detail about proteins. We did a texting poll which made Mr. Weber sort of upset because it didn't really work and so we had to do them the "old fashioned" way. We learned that proteins are made up of carbon, hydrogen, oxygen, nitrogen, and other small amounts of elements like sulfur. Amino acids are the monomers of proteins. They all share the same structure except for their variable R group. There are about 20 amino acids and they are group into non-polar, polar and acids and bases. We also talked about the structures of properties. those would be primary, secondary, tertiary, quartenary. Primary structures is just one string of amino acids held together by peptide bonds. Secondary structures is one polypetide folded into alpha helixes or beta sheets held together by hydrogen bonds. Tertiary structures fold into helixes and sheets and make a 3-d shape which is almost globular. Any protein could be quaternary if it consists of two or more polypeptides. 

 

9/17/10: Today we touched upon proteins again, and reviewed what we learned from wednesday. But today we touched mostly upon tertiary structures and their bonds. They have such a unique shape because of the four types of bonds that they have. Those would be electrostatic interactions, the SH bonds, covalent bonds and Van der wals forces. Dr. Weber had a little bit of a moment because he forgot that we already said the four types of bonds they made and we were afraid that there was one more, but it was actually very funny. Most of the class we talked with a partner about an experiment about tertiary structure proteins. This experiment wanted to test to see if there was a chemical inside the protein that helped keep its shape. To do this, they took purified ribonuclease and added things such as urea to break the bonds. Then they did a chromatography to separate the ribonuclease from the urea and other chemicals. When the urea was added, the bonds in the tertiary structure did break, and when it was separated, the bonds formed back together. So the hypothesis was supported because the protein did not need the help o outside forces to bond back together, so there must be something inside the protein that helps bond with itself to keep its hydrophobic parts in. 



 

B.  Useful Materials

 

http://www.nature.com/news/2010/100407/full/464828a.html

This article talks about how almost every human protein contains sticky segments that can lead into the formation of amyloids. When proteins become amyloids the sticky elements of the protein emerge and promote growth of deadly fibrils. These fibrils are known to be linked to Alzheimer's disease. This is an article that says evolution has helped these sticky segments stay apart from each other. The article talks about how its folded 3-d structure buries the amyloid prone segments, and that is how most proteins protect themselves from it.

 

 

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This video is a review and sort of the image of the different structures of proteins. There are four types of protein structures. Primary, secondary, tertiary and quaternary. Proteins are made up of a sequence of amino acids (can be an order of any of the twenty) held together by peptide bonds and folded into 3-d structures or added together to make one quaternary structure. 

 

http://www.sciencedaily.com/releases/2010/09/100908191132.htm

This article talks about how yeast can help researchers in the discovery of a new therapeutic drug that can treat Parkinson's disease. Yeast is used because they have biomedical pathways similar to that of the human body. Parkinson's disease is related to the death of dopamine producing neurons in the brain. These cells usually contain low protein deposits called Lewy Bodies. One small protein inside them is alpha-synclein, which is known to lead to cell death if there becomes an increased amount of it. 

Comments (2)

Derek Weber said

at 3:54 am on Sep 16, 2010

9/15: Updated.

Derek Weber said

at 4:18 am on Sep 23, 2010

This is a model page. Your blog about last Friday's class was spot on.

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