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CH. 1 THE CHEMICAL LEVEL OF ORGANIZATION
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REVIEW OF Ch. 1 1 a-d. Identify the indicated regions of the body. 1a. 1b. 1c. 1d.
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2. What is the primary organ found in the right hypochondriac region? 3. Name an organ found in hypogastric region?
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4. When the response to the effect of a stimulus is in the opposite direction it is called _______________ Feedback.
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CH. 2 THE CHEMICAL LEVEL OF ORGANIZATION 2.1 Elements and Atoms– the Building Blocks of Matter A. Matter : States of matter: B. Energy : 1. Types
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2. Forms of Energy (Text pp. 62-63) Chemical: Electrical: Mechanical: Radiant or electromagnetic
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C. Elements & Compounds Elements: 92, others created Atomic Symbol 4 elements = 96% of body
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Major Elements: Trace Elements Derived from: Text Page 51
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Elemental Deficiencies Iron (Fe): anemi Iodine (I): goiter
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D. Atoms & Subatomic Particles 1. Atom = 2. Atomic Structure & Energy Nucleus Protons (p + ) Neutrons (n 0 ) Electrons (e - ) Figure 2.1 E. Atomic Number & Mass 1.Atomic Number: # electrons 2.Atomic Mass TEXT PAGE 25
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Examples
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F. Isotopes (text p. 53) Protons: Neutrons: Symbol: H-1 or ¹H Atomic weight -- Figure 2.3
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Radioisotopes *Radioisotope: Radioactivity—process of spontaneous atomic decay PET Scan using glucose
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G. IONS (Text pp. 57-58) Cations Anions Importance: Know: atoms tend to want 2 or 8 electrons in their outer shell; Omit details on electron shells Example ATOMION Na Na+ = Cation
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IONS … Anions ATOM ION Cl Cl-
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IONS & IONIC COMPOUNDS Opposite charges attract each other ATOMS IONS Ionic Compound Na ClNa+ Cl-
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2.2 Chemical Bonds Bonds: Molecules Compound Figure 2.4
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A. Ions and Ionic Bonds Figure 2.6, step 2 Sodium atom (Na) (11p + ; 12n 0 ; 11e – ) Chlorine atom (Cl) (17p + ; 18n 0 ; 17e – ) Cl Na
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Crystals Figure 2.6, step 3 +– Sodium atom (Na) (11p + ; 12n 0 ; 11e – ) Chlorine atom (Cl) (17p + ; 18n 0 ; 17e – ) Sodium ion (Na + )Chloride ion (Cl – ) Sodium chloride (NaCl) ClNaCl Na cationanion
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B. Covalent Bonds: Figure 2.7a
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2 Types of Covalent Bonds 1. Non-polar covalent: 2. Polar bonds: Polar Molecule: Why chemicals dissolve in water: Figure 2.8
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Example: double bond ( Text p. 52) Figure 2.7b
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Comparison of Ionic, Polar & Nonpolar Covalent Bonds Figure 2.9
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C. Hydrogen Bonds (p. 35) Figure 2.9 Between: Molecules/compounds, not individual atoms in one molecule or compound Created by: Polarity Strength of Bond:
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2.3 Chemical Reactions A. The Role of Energy in Chemical Reactions - chemical energy Figure 2.10a
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B. Characteristics of Chemical Reactions - Reactants - Products - Chemical Equations Na + Cl NaCl Figure 2.10a Sodium atom (Na) (11p + ; 12n 0 ; 11e – ) Chlorine atom (Cl) (17p + ; 18n 0 ; 17e – ) Sodium ion (Na + )Chloride ion (Cl – ) Sodium chloride (NaCl) ClNaCl Na
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C. Types of Chemical Reactions 1. Synthesis Reactions Figure 2.10a
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2. Decomposition Reactions: Figure 2.10b
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3. Exchange reaction (AB + C AC + B) Figure 2.10c
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D. Reversibility of Chemical Reactions A + B ---- AB Changing the concentration of one or more chemicals in the reaction affects the direction of the reaction. If increase concentration of a chemical on one side, makes reaction go more to the opposite side (more of the chemicals on the opposite side are made). If decrease the concentration of a chemical on one side, makes reaction go more to that same side (more of the chemicals on the same side are made). Example: H 2 CO 3 ----- HCO 3 - + H+ -If more H+ (acid) is added, then more Carbonic Acid (a weak acid) is produced -If decrease H+ by adding OH- (they react to produce water), then makes more bicarbonate and H+.
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E. Factors Influencing the Rate of Chemical Reactions Temperature Concentration Pressure Catalysts - Enzymes
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2.4 Inorganic Compounds Essential to Human Functioning Types of Chemicals Organic compounds: Examples: Biochemicals Inorganic compounds:
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2.4 Inorganic Compounds Essential to Human Functioning A. WATER = 60-80% Functions Lubricant/cushioning Heat Sink Chemical Reactions ( text p. 59) Dehydration Synthesis Hydrolysis Solvent of living things Solutioins Solvent Solute Concentration of Solutions: % solute = (amount solute) (total amount) X 100%
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*Colloids *Suspensions
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B. SALT: ionic compounds not having H+ or OH- C. ACIDS and BASES 1. Have H+ and OH- 2. Proton (H+) donors and acceptors 3. pH pH scale
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Figure 2.12 4. BUFFERS—chemicals that can regulate pH change Are composed of a weak acid and its weak base Example: Carbonic acid—Bicarbonate system H 2 CO 3 ----- HCO 3 - + H+ If H+ is added to the solution: If OH- is added to the solution:
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2.5 Organic Compounds Essential to Human Functioning Carbon & Covalent Bonding Macromolecules Polymers and Monomers: Functional Groups Text page 64, Table 2.1 A. Carbohydrates 1. Elements: 2. Functions: ATP Cell Recognition 3. Saccharides = Sugars
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4. Three Forms Monosaccharides Examples (Text p. 65) Disaccharieds Examples (Text p. 66) Polysaccharides Examples (Text p. 67)
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5. Isomers Isomers Glucose Glucose
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7. Combined w other biochemicals Glycolipids Glycoproteins Lipid Galactose Glycolipid
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B. Lipids 1. Contain Elements: Ratio 2. In water 3. Functions:
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4. Types Triglycerides = Neutral Fats Composition Saturated vs. Unsaturated vs. Trans Fats Omega-3 fatty acids Phospholipids = Function Steroids Prostaglandins P
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C. Proteins 1. Subunit = Elements: NH 2 (amine) and COOH (carboxyl) R- group: 2. Peptide Bond: dehydration synthesis Figure 2.16 Structure of amino acid R
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3. Structural Levels of Proteins (Text p. 73) Figure 2.18a–c Secondary tend to be fibrous and so form structures Primary = the sequence of amino acids. Proteins do not remain in this form
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Structural Levels of Proteins … Figure 2.18b,d,e Tertiary have a unique shape that is important to their function
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4. Protein Denaturation = Figure 2.19b
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5. over half body’s organic matter 6. Combine with other biochemicals Glycoproteins & Proteoglycans Lipoproteins 7. Functions: Build Structures Hormones Carry Oxygen & Carbon Dioxide Buffers Transport substances across the cell membrane Enzymes details next slide Hemoglobin Collagen
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7. Enzymes and Enzyme Activity Enzymes = General Function–Catalyst Characteristics of Enzymes Shape Recycling Cofactors Coenzymes “ase” ending Mechanism of Action Next Slide Enzyme Reactants Products
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Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Substrates (S) H2OH2O + Mechanism of Enzyme Activity ( Steps on pp. 74) Substrate Active Site Energy of Activation
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Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Internal rearrangements leading to catalysis Substrates (S) H2OH2O +
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Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Internal rearrangements leading to catalysis Dipeptide product (P) Free enzyme (E) Substrates (S) Peptide bond H2OH2O +
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D. Nucleic Acids (Text pp. 74-76) 1. Nucleic Acids = 2. Types: DNA and RNA 3. Elements 4. Nucleotides: Phosphate Monosaccharide Nitrogenous Base Purines: Adenine and Guanine Pyrimidines: Cytosine, Thymine, and Uracil 5. Dehydration Synthesis: sugar of one nucleotide to phosphate of another nucleotide 6. Overview of DNA and RNA
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DNA Nitrogenous Bases: A, G, C, T Sugar = Double Helix Complementary bases Function RNA Sugar = U replaces T Single stranded Function Released mRNA
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Function: -Hydrolysis of phosphates Food + O2 + ADP + Pi ATP + CO2 -Phosphorylation ATP + H2O ADP/AMP + Pi + Energy energy transfer energy released 7. Other Related Chemicals Adenosine Triphosphate (ATP) (Text p. 77)
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Figure 2.21 + ADP Solute Contracted muscle cell Product made Relaxed muscle cell Reactants Transport work Mechanical work Chemical work Membrane protein Solute transported Energy liberated during oxidation of food fuels used to regenerate ATP ATP P P P X Y (a) (b) (c) YX P P + Adenosine Triphosphate (ATP) … Released Energy is used for:
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END
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REVIEW QUESTION 1. What is the atomic number and atomic mass of each of the above atoms?
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4.What sort of chemical reactions do you suppose would be happening during digestion? What about when your body is making more bone? Review Question
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5. What are the 4 major groups of biological organic molecules? What is a major function of each? Review Question
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REVIEW QUESTION What are 2 variables that can distort the active site of an enzyme and what is the distortion process called? Dysfunctional Enzyme
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