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Biology 243 Chapter 2 Notes

by: Karla Kristo

Biology 243 Chapter 2 Notes BIOL 243

Marketplace > University of South Carolina > Biology > BIOL 243 > Biology 243 Chapter 2 Notes
Karla Kristo

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Chemistry Comes Alive
Human Anatomy and Physiology I
Lewis Bowman
Class Notes
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This 6 page Class Notes was uploaded by Karla Kristo on Wednesday September 7, 2016. The Class Notes belongs to BIOL 243 at University of South Carolina taught by Lewis Bowman in Fall 2016. Since its upload, it has received 7 views. For similar materials see Human Anatomy and Physiology I in Biology at University of South Carolina.

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Date Created: 09/07/16
Chapter 2: Chemistry Comes Alive: Part A Matter  liquid, solid, gas – occupies space and has matter Energy  no mass, capacity to do work Living things comprised of matter and require energy to grow and function Convert food into useable energy Two components of energy: 1. Potential energy  energy something has due to its position or structure 2. Kinetic  associated with movement of matter a. Heat major part Forms of energy 1. Chemical energy  stored in chemical bonds a. When bonds are broken released as kinetic energy 2. Electrical energy  associated with movement of charged molecules 3. Mechanical energy  moving matter 4. Radiant/ Electromagnetic  energy like light, ultraviolet, radio waves, x-rays Element  pure chemical substances single type of atom C,O,N,H Atom  smallest part of element; surprised of subatomic particles Contains nucleus with neutrons (neutral) and protons (positive) Electrons on each energy level – 2,8,8 Number of electrons = number of protons Reactivity  determined by the number of electrons on the outer energy level (valence shell)  Atoms interact to complete energy level  Inert elements unreactive Bonds Ionic bonds  complete transfer of electrons from one atom to another (forming IONS) and will be charged Covalent bonds  share electrons Share one pair of electrons  single bond (--) Share two pairs of electrons  double bond Nonpolar covalent bonds  electrons are shared equally Polar covalent bonds  electrons are unequally shared, generates regions of pos. and neg. charge Hydrogen bonds  weak bonds H bonds to electronegative element (O,N) is attracted to a electronegative element H+  - Biochemistry H2O  Water has high heat capacity  High heat vaporization (amount of energy put into water to convert liquid to gas)  Solvent because of polarity of H2O, both neg. and pos. charge molecules interact with H2O  Makes water good transport medium  Uncharged molecules do not dissolve in H2O  Reactivity   Cushioning  Organic Molecules (C)  Carbon forms covalent bonds  Can form bonds with four other atoms  Complicated molecules Carbohydrates  Monosaccharide  basic building blocks, contain C, H, O (1:2:1 ratio) exist as ring or a chain – 3-7 carbons  Disaccharides  two monosaccharide’s joined together o Sucrose = glucose + fructose (common table sugar) o Lactose = galactose + glucose o Maltose = glucose + glucose  Polysaccharides  large branching polymers of linked monosaccharide’s o Glycogen – glucose – animals o Starch – glucose - plants o Glycogen can be broken down to glucose, glucose + oxygen produces CO2 + H2O = release energy Functions of Carbohydrates  Energy  Structure  outside layer of cell is lined with carbohydrates High fructose corn syrup = Start with corn syrup (high % glucose) modified to change levels of fructose to be higher Lipids  Not defined by a specific structure but by solubility  Organic molecules that are insoluble in water  Non polar molecule covalent bonds  Class of lipids 1. Triglycerides = glycerol + 3 fatty acid chains a. Saturated; only single bonds in the tail of the fatty acids i. Animal fats – chicken, beef, butter ii. Insoluble at room temperature, solid b. Unsaturated; one or more double bonds i. Vegetable oil, corn oil, olive oil ii. Liquid at room temperature Functions of triglycerides o Energy source  Double the amount of calories or energy of carbohydrates; 2x cal of per gram of carbs o Insulation o Protection  surrounds organs (fatty capsules) ex. Surrounds kidney so can be protected in fat Triglycerides containing saturated fatty acids (all single bonds; animal fats  like butter and fat from meats) and triglycerides containing unsaturated  fatty acids  (one or more double bond; plant oils like canola or olive oil) are both  insoluble in water.  They are lipids, and all lipids are insoluble in water. Triglycerides containing saturated fatty acids are solid at room  temperature, whereas triglycerides having at least one unsaturated fatty  acid are a liquid at room temperature. 2. Phospholipids = glycerol + two fatty acid tails + phosphorus (P) containing group = charged a. Similar to triglycerides b. Bilayer (polar head with nonpolar tail) c. Backbone of cellular membrane 3. Steroids = cholesterol structural building blocks for steroids a. Female – estrogen b. Males – progesterone Proteins = long polymers of amino acids linked together a. Amino acids are basic building blocks b. 20 amino acids (20 R groups) c. R groups can vary (small, large, acidic, basic, nonpolar, polar) d. Amino acids are linked by peptide bonds to make proteins e. Polypeptide – one chain of amino acids (any length) Structure of Proteins 1. Primary structure  sequence of amino acids forms the polypeptide chains a. Contains information for the secondary, tertiary and quaterinary structures 2. Secondary structure  region or part of polypeptide; primary chain forms spirals (a helices) – H bonds and sheets (B sheets) 3. Tertiary structure  overall 3D structure of one polypeptide 4. Quaternary structure  some proteins consist of more than one polypeptide; arrangement of two or more polypeptide  **Structure of protein is essential for function o Unfolding (denaturation) o Reasons: pH, heat, etc o Ex. Sickle cell due to change in one amino acids in hemoglobin ; Red blood cells form in shape of sickle and get clogged in arteries and capillaries Types of Proteins  Fibrous – structural protein o Collagen (found in bones, skin, connective tissue and helps hold together) o Keratin ( skin, looks like rope)  Functional proteins o Globular (look like glob,) a) Hormones b) Antibodies (proteins which react with other proteins, immune system) c) Enzymes (biological catalysts; accelerate the rate of a chemical reaction but are not used up)  25,000 genes  code for 1 polypeptide  Highly specific  1 enzyme for 1 type of chemical reaction  Lower the energy of activation (lower the amount of energy needed to begin a chemical reaction)  All chemical reactions speed downhill o Reactants have higher energy than product; it has less energy at end of reaction o Lower activation energy required (enzymes) so reaction moves quicker (mechanism of enzyme action)  Substrate – reactant  Active site on enzyme  Substrate binds to active site on enzyme, reaction takes place on enzyme; reactants will bind to enzyme  Rearrangement  reaction takes place  Product is released  Strucutre of DNA  Nucleic acids: Nucleotides  basic building block of nucleic acids (linked in chain) 3 parts: 1. 5 Nitrogenous base Adenine (A) Guanine (G) Cytosine (C) Thymine (T) Only found in DNA (has methyl group which U does not) Uracil (U) Only found in RNA 2. Sugars: Deoxyribose  DNA Ribose  RNA 3. Phosphate Group Phospate  phosphodiester bond connects nucleotides Sugar base back bone is line with sugars coming of  DNA o Double strands o H- bonds hold strands together o A= T o G=C o Genetic material contains information for sequence of amino acids in proteins  RNA o Single stranded o Decoding information in DNA o A=U


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