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by: Osei Kuffour


Osei Kuffour

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This study guide to help all students to solve all their chemistry problems.
Fundamentals Chemistry I
Study Guide
MCAT General Chemistry, Organic Chemistry, General Chemistry
50 ?




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This 9 page Study Guide was uploaded by Osei Kuffour on Wednesday August 10, 2016. The Study Guide belongs to CHEM 1030 - 013 at Auburn University taught by TBA in Fall 2016. Since its upload, it has received 206 views. For similar materials see Fundamentals Chemistry I in Organic Chemistry at Auburn University.




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Date Created: 08/10/16
Pierce College Putman/Biol 241 Lecture 2: Chemistry notes General Chemistry 1. Universe is made of matter (physical substance) + energy A. Matter is made of atoms B. Atoms “glued” together by 2. Ionic Bonds: A. Atoms from far left (low electronegativity) and far right ( ) 1) exchange electrons, increasing stability: Filling outer shells 2) E exchange produces ions 3) Ionic bond = attraction B. Atoms held loosely by charge C. Water can separate D. Electrolytes E. Physiological importance? 3. Covalent Bonds: A. CHNOPS B. E sharing increasing stability, filling 1) Why doesn’t electron exchange occur? 2) Electronegativity difference C. Atoms held tightly D. Water can’t separate E. Not electrolytes! F. Physiological importance? G. Pure Covalent Bonds 1) Between at+ms wi-h identical electronegativities a) No  or  regions, thus not “sticky”; gas at room temperature! 2) May form very stable structures (carbon-carbon bonds) H. Polar Covalent Bonds 1) Between atoms with different electronega-ivities. a) Example, in water, oxygen pulls e s more strongly than hydrogen b) Results in oxygen with  , hydrogen with  + c) Thus molecule can be “sticky” Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 1 4. Hydrogen Bonds A. We+k but significant bond - B.  of a hydrogen attached to oxygen (or nitrogen) of one molecule attracts  of oxygen (or nitrogen) of another molecule C. Why only oxygen (or nitrogen)? Electronegativity D. Importance of hydrogen bonds 1) Hold macromolecules together 2) Cohesion and adhesion a) Cohesion is? b) Adhesion is? c) Increases viscosity of blood; smaller vessels, higher surface area, more hydrogen bonding, heart works harder! 1. Explains blood pressure. 3) High heat of vaporization of water a) Hydrogen bonds absorb heat energy before breaking b) Evaporative cooling 4) Allow water to be solvent a) Bonds and wiggles stuff into solution! b) Plasma and lymph are aqueous solutions c) Solvents dissolve solutes into solution d) H and OH ? - + - 5) Water solubilizes “loose” H and OH a) Allows for the formation of acids (H ) and bases (OH ) - 5. pH A. Measure of “loose” hydrogen ions in aqueous solution B. Importance: Affects how enzymes work! + C. pH = -log [H ] 1) Distilled water = “neutral” pH a) Where [H ] = [OH ] = 10 moles/L b) pH = 7 + D. Acids give up H into aqueous solution 1) [H ] > 10 -7 E. Bases absorb (remove) H from aqueous solution + -7 1) [H ] < 10 - 2) By contribution OH or NH 3 F. Physiologically important pH values: 1) Concentrated HCl 1.0 2) Gastric juice 1.2-3.0 Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 2 3) Vaginal fluid 3.5-4.5 4) Urine 4.6-8.0 5) Saliva 6.35-6.8 6) Pure water 7.0 7) Blood 7.35-7.45 8) Semen 7.20-7.60 9) Cerebrospinal fluid 7.4 10)Pancreatic juice 7.1-8.2 11)Bile 7.6-8.6 12)Lye 14.0 6. BICARBONATE BUFFER SYSTEM A. In all body fluids: B. Buffers maintain constant pH in aq+eous solutions 1) Absorb or release H+ when H are added or removed from system. C. The bicarbonate buffer system maintains a plasma pH at 7.35 to 7.45; a pH above this leads to alkylosis; a pH below this leads to acidosis. D. System: Carbon dioxide combines with water to form carbonic acid. Carbonic acid dissociates into a hydrogen ion (proton) and bicarbonate, bicarbonate dissociates into a second hydrogen ion plus carbonate: + - + -2 CO 2 H O2 H CO 2H +3HCO  H + CO 3 3 1) The addition of acid (H ) causes equilibrium to move to the left; this means that the hydrogen ions combine with the carbonate, forming bicarbonate, and with the bicarbonate forming carbonic+acid, which dissociates into carbon dioxide and water— thus the concentration of H stays constant. 2) The removal of hydrogen ions, which would happen if a base were added, causes carbonic acid to dissociate, forming more hydrogen ions, and bicarbonate, bicarbonate then possibly disso+iating into hydrogen ion plus carbonate, thus, again, keeping the concentration of H constant. BIOCHEMISTRY 1. The chemistry of biological molecules 2. Chemical reactions of metabolism A. Metabolism: The sum total of the biochemical reactions in body. B. Anabolic Reactions 1) Make bonds (synthesis) 2) Usually endergonic; energy absorbed into the formation of chemical bonds. C. Catabolic Reactions. 1) Break bonds (decomposition rxns) 2) Usually exergonic; energy released in the breaking of chemical bonds. Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 3 D. Energy Diagrams 1) Anabolic Rxns 2) Catabolic Rxns E. Chemical reactions require a bit of energy to force the formation of a highly unstable transition state. Once this transition state is formed, it spontaneously falls apart either into products or back into the original reactants. The energy required to force the transition state is called the energy of activation. Catalysts, such as enzymes, reduce the activation energy, thus speeding up the chemical reaction. F. If the energy contained in the reactants is greater than the energy of the products, the reaction releases energy and is thus exergonic. If the energy contained in the reactants is less than the energy of the products, the reaction takes in energy and is thus endergonic. 3. Two important biochemical reactions A. Dehydration synthesis B. Hydrolysis Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 4 4. MACROMOLECULES A. Introduction 1) Are polymers of monomers 2) Made by dehydration synthesis! B. CARBOHYDRATES 1) Monomers: Monosaccharides a) Hydrophilic. Why? b) Examples: 1. Glucose (= Dextrose) a. Blood sugar b. Energy for body 2. Galactose 3. Fructose a. Stored as fat b. Increase insulin resistance; bad for diabetics c. Major health concern c) Monomers directly absorbable by body; don’t need to be digested. Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 5 2) Disaccharides -Must be digested to be absorbed by body! a) Maltose 1. “Malt sugar” 2. Glucose + glucose joined by  glycosidic lineage a. Humans have  glycosidases b) Sucrose 1. “Table sugar” 2. Glucose + fructose joined by  glycosidic lineage c) Lactose 1. “Milk sugar” 2. Galactose + glucose joined by  glycosidic lineage a. Most humans stop producing  glycosidases in childhood b. Thus lactose intolerance 3) Polysaccharides -Must be digested to be absorbed by body! a) Glycogen 1. Chains of -linked glucose 2. Branches every 8 residues, thus granular. 3. “Animal starch” b) Starch 1. Amylopectin a. Chains of -linked glucose b. Branches every 20 residues, thus not granular. 2. Amylose a. Chains of -linked glucose b. No branches c) Cellulose 1. Chains of -linked glucose 2. No branches 3. “Fiber” d) Chitin 1. Chains of -linked modified glucose 2. No branches 3. “Animal fiber” Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 6 C. LIPIDS 1) Fats, oils, waxes 2) Generally hydrophobic 3) Tryglicerides a. Glycerol + three fatty acids b. Saturated vs unsaturated fatty acids 1. Saturated a. All single-bonded carbons b. Regular, compact structure; solid at blood temp c. Increases risk of heart disease 2. Unsaturated: a. One or more double bonds b. Irregular structure; liquid at blood temp c. Decreases risk of heart disease c. Function of triglycerides? 4) Phospholipids a. Glycerol + two fatty acids + phosphate group b. Hydrophilic part, hydrophobic part c. Function: 5) Sterols a. Synthesized from cholesterol b. Function of sterols? c. Representative sterols D. PROTEINS 1) Monomers: a) Structure 1. Amine 2. Carboxylic acid 3. R group b) Representative amino acids 2) Four levels of protein structure a) PRIMARY 1. Peptide sequence b) SECONDARY 1. Helix and/or folding c) TERTIARY 1. Helix and/or folding Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 7 d) QUATERNARY 1. Two or more 3 structures 3) Two types of proteins a) Fibrous 1. Examples: Collagen, keratin 2. Functions: b) Globular 1. Example: Enzymes, hemoglobin 2. Functions: 4) Denaturation a) Irreversible change in shape b) Must be correct shape to work/fit with other molecules c) Shape changed by 1. pH 2. Temp 3. Salt conc 4. Pressure 5) Enzymes a) Work by lowering Ea of a reaction; takes less energy to form transition state! 1. Increase rate of reaction b) Structure: 1. Holoenzyme is entire enzyme 2. Apoenzyme (protein) a. Shape (activity) affected by? 3. Coenzyme/cofactor activate enzyme b. Vitamins/minerals c) Mechanism of catalysis: How do enzymes work? 1. Substrate fits into active site of enzyme. 2. Hydrolysis or dehydration synthesis is forced a. Speed up chemical rxn 10 to 10 times by lowering the Ea, thus requiring less energy to achieve the transition state. 3. Product(s) released 4. Enzyme does it again; not used up in the reaction! E. NUCLEIC ACIDS 1) Monomeric unit: Nucleotide DNA RNA Location Function Single or Double Stranded? Sugars? Deoxyribose Ribose Bases? ATCG AUCG Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 8 2) Sugar? Base? Phosphate? Nucleotide? 3) ATP a) Function 1. Phosphorylates target molecule; causes target molecule to a. Fall apart b. Rearrange c. Combine with another molecule b) Regeneration? Putman/Pierce College Biol 241 Unit 02 Gen Chem Lecture Notes/20130521/Page 9


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