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Four Groups of Macromolecules: Recently the FDA gave its approval to Proctor and Gamble to use a controversial fat replacement in snack foods. What makes olestra unique is that it is not just a fat substitute, but it is a fat. It has all of the same properties of fat when it is used in cooking, but the body can not absorb it so it has no calories. At first glance, olestra sounds like the answer to the prayers of many dieters'. However, there are some serious pro's and con's that go with this story. Proctor and Gamble began developing and studying olestra 25 years ago. To date the company has spent a reported $200 million testing the product. Originally, the intent was to have olestra approved for use in many products, but the scope had to be narrowed to quicken the approval process. The company plans to use olestra in Pringles chips. It is estimated that the approval of olestra will generate an annual market of one billion dollars within the next ten years. The Pro's: •products taste very similar to the real thing •zero calories •no fat absorbed by the body •non- toxic The Con's: The arguments against olestra are strong as well. One less than pleasant side effect is diarrhea and in some individuals, something called "anal leakage". The Diarrhea is caused by the chemical structure of olestra. It is a large molecule with fatty acids packed very close together. The body's enzymes can not break down the fat and the molecule passes through the intestine unabsorbed. http://www.cheshire-med.com/services/dietary/nutrinew/olest.html Second Macromolecule Group: The Fats of Life: LIPIDS • Fats, oils, cholesterol, hormones • Composed of C,H,O but not water soluble • Store the most energy: these are energy storing molecules! Three types of fats 1. Triglycerides 2. Phospholipids 3. Sterols 1. TRIGLYCERIDES • Most common fat in plants and animals, used in storage • A molecule of 3 fatty acids attached to a glycerol backbone: fatty acid fatty acid fatty acid There are two types of triglycerides: 1) Saturated triglycerides -have single bonds, solid at room temperature -have straight chains 2) Unsaturated triglycerides -have double bonds, liquid at room temperature -have bent chains 2. PHOSPHOLIPIDS -structural components of cell membrane hydrophilic phosphate head hydrophobic tail Some cool things you can do with lipids… 3. STEROLS • Cholesterol is a natural component of cell membranes • used by cells to make steroid hormones, vitamin D, bile salt • if there is too much, cholesterol can close arteries, depriving tissue of nutrients and leading to stroke good cholesterol vs. bad cholesterol Cholesterol and blood do not mix well. So, for cholesterol to travel through your blood, it is coated with a layer of protein to make lipoprotein • You want to have low LDL (low density lipoprotein) and high HDL (high density lipoprotein cholesterol testosterone progesterone Third Group of Macromolecules: PROTEINS • The functional molecules – Help chemical reactions take place (ex. enzymes) – Repair and maintain the cell – Transport materials around the body – Ex. enzymes, hemoglobin, hair • Proteins are "unbranched polymers of amino acids" • Amino acids: small molecules containing a central C atom and a side chain – There are 20 amino acids in human food – 8 of those are essential: we do not produce them and therefore must EAT them • Amino acids link together during protein synthesis through peptide bonds to form a POLYPEPTIDE – Most functional proteins will contain hunderds and thousands of amino acids linked together • As the polypeptide lengthens it can fold into sheets (b-sheets) or wrap into coils (a-coils) • Protein function depends on its 3-dimensional shape Primary: specific amino acids join together using peptide bonds to form a polypeptide Secondary: the polypeptide forms ahelices or b-sheets Tertiary: polypeptides form and fold in a specific way, making extra bonds between parts of the protein Quarternary: two or more polypeptides assemble to form a larger protein Figure 3.9 Life 8e: Quaternary Structure of a Protein Hemoglobin consists of four folded polypeptide subunits that assemble themselves into the quaternary structure shown here. In these two graphic representations, each type of subunit is a different color. The heme groups contain iron and are the oxygen-carrying sites. • Both shape and chemistry allow a protein to behave in a specific way • Denaturation: – a change in the three-dimensional shape of a protein caused by high temperatures or harsh chemical conditions (ex. acids, bases, salts) • A denatured protein cannot carry out its original function positives negatives - fever: can denature bacteria - straightening/ curling hair - cooking meat - fever: can cause damage - if peptide bonds are broken protein will be destroyed Homework 1. Describe some groups of lipids that are not triglycerides. 2. What are the structural components of triglycerides? 3. How do saturated fats differ from unsaturated fats? 4. How can only 20 amino acids account for the many different proteins? 5. Define protein denaturation. Why is it important?