Biology Week 4 Notes
Biology Week 4 Notes BIO 103-002
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This 6 page Class Notes was uploaded by Lucas Kinsey on Monday October 3, 2016. The Class Notes belongs to BIO 103-002 at George Mason University taught by Gwendolyne Fondufe in Fall 2016. Since its upload, it has received 31 views. For similar materials see Introductory Biology I in Biology at George Mason University.
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Date Created: 10/03/16
Lucas Kinsey Biology 103 Week 4 Notes Chapter 2-3 Chapter 2 Organisms are composed of elements in combinations called compounds Oxygen, Carbon, Hydrogen, and Nitrogen make up about 96% of all living matter Iodine helps with thyroids Flouride helps with tooth protection Iron helps with blood flow - Compounds and elements combined with resources help organism health Radioactive isotopes, where the nucleus decays spontaneously, can be helpful or harmful to us - Can be used as tracers to moniter flow of nutrients - Radioactive iodine can kill cancer cells in the thyroid Alzheimer’s Disease - Happens when a brain becomes riddled with protein deposits called beta-amyloid o PIB is a protein that bonds to beta-amyloid and contains a radioactive isotope that can be detected on a PET scan Particles and energy thrown off by radioactive atoms can break chemical bonds and cause abnormal nonds to form in DNA and can cause cancer due to DNA mutation Salts are ionic compounds Hydrogen bonds are weak bonds important in the chemistry of life Cells are constantly rearranging molecules via chemical reactions Water is the solvent of life - Has the ability to dissolve nessesary components for life so cells can absorb such nutrients Biological fluids contain buffers that regulate pH in body and cells, they do so by accepting H+ when its in excess and donating H+ when it is depleted Chapter 3 Organic Compounds: carbon based molecules Carbon is a fundamental element for life because of its 4 electrons in an 8 valence electron shell. This allows for chemical bonds to occur. There are usually 4 hydrogen atoms attached to carbon - Uses covalent bonds - CH_4 forms a tetrahedron Carbon skeletons form the backbone of most organic molecules. Carbon skeletons vary in length, double bonds, branching, and rings Isomers: compounds with the same formula but different structural arrangements Hydrocarbons: compounds composed of only carbon and hydrogen Functional chemical groups affect a molecule’s function by participating in chemical reactions. They are polar which makes compounds hydrophilic (water loving) and therefore soluble I water Methyl chemical group is non polar and not reactive 4 Main Classes of Important Molecules for al Living Things: 1. Carbohydrates 2. Lipids 3. Protiens 4. Nucleic Acid Polymers: Macromolecules that are composed of joined smaller molecules into chains Monomers: building blocks of polymers - Basically small molecules form to make big molecules Polymers are made by dehydration reactions that remove a molecule of water as two molecules become bonded together Hydrolysis: the digestion of polymers to access energy - Basically the opposite of dehydration Both dehydration reactions and hydrolysis require the help of enzymes to make and break bonds Enzymes: specialized macromolecules that speed up chemical reactions in cells Small molecules common to all organisms are ordered into large molecules, which vary from species to species and even from individual to individual in the same species - Structure and Function inseparable Carbohydrates Monosaccharides: Simple sugars and are the monomers of carbohydrates - EX: glucose and fructose - Generally have a molecular formula that is a multiple of CH 2 Disaccharide: when 2 monosaccharides are linked together via a dehydration reaction Polysaccharides: polymers of A LOT of monosaccharides put together 3 Main Types of Polysaccharides: 1. Starch: a. A starage polysaccharide, consists of long chains of glucose monomers b. Energy banks for plants c. Humans have enzymes that turn starch into glucose 2. Glycogen: a. Where animals store glucose b. Stored in liver and muscle cells 3. Cellulose: a. Most abundant organic compound on earth b. Compound that gives strong cell walls to plant cells Lipids All lipids do not mix well with water, or rather, they are all hydrophobic (anti water) 3 main types of Lipids: 1. Fats: a. Made from 2 kinds of smaller molecules: glycerol and fatty acids b. Triglyceride: s synonym for fat, and a term that refers to fat in blood c. Unsaturated fatty acid: a hydrocarbon chain that contains one or more double bonds d. Saturated Fatty Acid: a fatty acid that has no double bonds in its hydrocarbon chain e. Most animal fats are saturated, therefore packing them closer together and allowing them to solidify at room temp f. Trans fats: a form of fat that recent research associates with health risks g. When converting unsaturated fat to saturated fat, hydrogen is added through a process called hydrogenation and creates trans fats as a sub product h. **The main function of fats is for long term energy storage i. Fat stored in specialized reservoirs in humans called adipose cells 2. Phospholipids: a. Phospholipids are structurally similar to fats except that they contain only 2 fatty acids attached except that they conaint only 2 fatty acids attached to glycerol, insteadrdf 3 and have a phosphate group attached to glycerol’s 3 carbon b. Cells cannot exist without phospholipids, they line cell membranes and have hydrophilic heads facing outwards and hydrophobic tails facing inwards 3. Steroids: a. Lipids in which the carbon skeleton contains four fused rings b. Cholesterol is common in animal cell membranes and is also the precursor for making other steroids, including sex hormones c. Anabolic Steroids: synthetic variants of the male hormone testosterone Proteins Protein: a polymer of small building blocks called amino acids - Nearly every dynamic function in your body involves proteins Enzymes: chemical catalysts that speed and regulate virtually all chemical reactions in your cells Proteins can be used as enzymes to transport agents, defensive antibodies, signal proteins, receptor proteins that transmit signals to cells, contractile proteins and structural proteins in muscles, and storage proteins which supply amino acids The structural protein collagen makes up 40% of protein in the body Lysozyme: an enzyme found in sweat, tears, and saliva Nearly all proteins must recognize and bind to some other molecule to function Denaturation: a process where a protein unravels, losing its specific, and as a result, its function Newly synthesized amino acids quickly fold into functional shape - Misfolds create diseases such as Alzheimer’s and Parkinson’s Proteins are made from amino acids linked by peptide bonds Amino acid polymers are created via a dehydration reaction. The resulting bond is called peptide bond, which is a covalent bond Polypeptide: an amino acid chain with multiple peptide bonds - Each one has a unique sequence of amino acids, some with more than 1000 Primary structure of a protein: the precise sequence of amino acids in the polypeptide chain Nucleic Acids Amino acid sequence of a polypeptide is determined by genes - DNA = Deoxyribonucleic acid DNA provides directions for its own replication - RNA = Ribonucleic Acid Nucleic Acids are polymers of nucleotides 4 Nitrogenous bases: 1. Adenine 2. Thymine 3. Cytosine 4. Guanine RNA uses same nitrogenous bases except uses Uracil instead of Thymine
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