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Anatomy and Physiology I (BSCI 201)- Chapter 2 notes- part 2

by: mehrnazighani Notetaker

Anatomy and Physiology I (BSCI 201)- Chapter 2 notes- part 2 BSCI201

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Chapter 2: Basic Chemistry and Biochemistry
Human Anatomy and Physiology 1
Justicia Opoku-Edusei
Class Notes
anatomy, anatomy&physiology, Physiology, Science, Chemistry, biochemistry, equations, Proteins, Enzymes, functions, structure
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This 7 page Class Notes was uploaded by mehrnazighani Notetaker on Thursday September 15, 2016. The Class Notes belongs to BSCI201 at University of Maryland - College Park taught by Justicia Opoku-Edusei in Fall 2016. Since its upload, it has received 45 views.


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Date Created: 09/15/16
Chapter 2: Basic Chemistry and Biochemistry- Part 2 by Mehrnaz Ighani .3 main types of chemical reactions: 1. Synthesis reactions: atoms/ molecules combining to form larger molecules (Fig. 2.11a) ­ Used in anabolic processes A+ B AB 2. Decomposition reactions: breakdown of a molecule into smaller molecules (Fig. 2.11b) ­ Used in catabolic processes such as the conversion of glycogen to glucose ABA+B 3. Exchange reactions: (Aka displacement reactions) involve both synthesis and decomposition reactions (Fig. 2.11c) ­ Bonds are broken and formed AB+CDAD+CB Example: acid+ base water +salt . In living systems, reduction-oxidation or redox reactions are critical, atoms are reduced when they gain an electron and oxidized when they lose an electron ­ Ex. Glucose+ oxygen carbon dioxide+ water+ ATP Oxygen is reduced and glucose is oxidized . All chemical rxns are either exergonic or endergonic: 1. Exergonic: net release of energy, products have less potential energy than reactants ­ Example: catabolic and oxidative rxns 2. Endergonic: net absorption of energy, products have more potential energy than reactants ­ Example: anabolic rxns . All chemical rxns are reversible: A+ B ↔AB ­ Chemical equilibrium occurs if neither a forward nor a reverse rxn is dominant . Many biological rxns are not very reversible because energy requirements to go backward are too high or products have been removed . The rate of chemical rxns can be affected by: 1. Temperature: ↑ temperature means ↑ rate of rxns 2. Concentration of rxns: ↑ concentration means ↑ rate rxns 3. Particle size: smaller particles, ↑ rate of rxns 4. Catalysts/ enzymes: increase the rate of rxns without being consumed or altered . Biochemistry: the study of chemical composition and reactions of living matter . All chemicals are either organic or inorganic: 1. Inorganic compounds: water, salts, acids, and bases (don’t contain chains of C) 2. Organic compounds: carbs, proteins, fats, and nucleic acids (contain chains of C, covalently bonded) . Inorganic compounds: ­ Water is the most abundance inorganic compound composing 60- 80% of the volume of living cells ­ Water is important due to its properties: 1. High heat capacity 2. High heat of vaporization 3. Polar solvent properties: dissolves and disassociates ionic substances and it’s body’s major transport medium 4. Reactivity: needed for hydrolysis and dehydration 5. Cushioning: protects organs from physical trauma ­ Salts: ionic compounds that disassociate into separate ions in water ­ Acids and bases are electrolytes that disassociate and ionize in water  Acids: proton donors o Release H ions o Important acids: HCl, carbonic acid, and acetic acid  Bases: proton acceptors o Pick up H ions o When a bases dissolves it releases a hydroxyl ion (OH) o Important bases: bicarbonate ion and ammonia ­ pH scale: measurement of concentration of H ions in a solution (Fig. 2.13)  high H ions results in low pH  pH is – log of H ions in moles/liter that ranges from 0-14  pH scale is logarithmic, so each pH unit represents a 10 fold difference  Acidic (0-6.99), basic (7.01-14) . Neutralization rxn: acids and bases are mixed ttogether NOTE: Acidity involves only free H ions in a solution, not H ions bound to anions . Buffers: resist abrupt and large swings in pH  Release H ions if pH increases (becomes basic)  Bind H ions if pH decreases (becomes acidic)  Convert strong acids or bases into weak ones . Organic compounds: ­ Contain chains of C except CO2 and CO which are inorganic ­ Carbon is electroneutral : o Shares electrons o Forms 4 covalent bonds ­ Major organic compounds: 1. Carbohydrates 2. Lipids 3. Proteins 4. Nucleic acids ­ Synthesized by dehydration synthesis and broken down by hydrolysis rxns (Fig. 2.14)  Carbs: o Sugars and starches that contain C, H, and O o 3 classes: 1. Monosaccharides: single sugars (monomers: smallest unit of carb) 2. Disaccharides: 2 sugars 3. Polysaccharides: 3 sugars o Monosaccharides: (Fig. 2.15a)  Simple sugars containing 3-7 C atoms  General formula (CH2O)  Important monosaccharides: Pentose sugars: Ribose and deoxyribose Hexose sugars: Glucose, fructose, and galactose o Disaccharides: (Fig. 2.15b)  Double sugars that are too large to pass the cell membrane  Formed by dehydration synthesis of 2 monosaccharides  Important disaccharides: Sucrose: glucose+ fructose (table sugar) Lactose: glucose+ galactose (milk sugar) Maltose: glucose+ glucose (grain sugar) o Polysaccharides: (Fig. 2.15c)  Polymers of monosaccharides that are not very soluble  Important polysaccharides: Starch (in plants) Glycogen (in animals)  Lipids: ­ Contain C,H,O, and sometimes P ­ Hydrophobic ­ Main types: 1. Triglycerides/ neutral fats 2. Phospholipids 3. Steroids 4. Eicosanoids o Triglycerides: Called fats when solid and oils when liquid Composed of 3 fatty acids bonded to a glycerol molecule Used for energy storage, protection, and insulation Can be constructed of:  Saturated fats: Solid at room temp. All Carbons linked via single covalent bonds Molecules with the highest # of H atoms Ex. Animal fats, butter  Unsaturated fats: Liquid at room temp One or more carbons are linked via double bonds resulting in low # of H atoms Ex. Olive oil Trans fat: modified oils (unhealthy) Omega-3 fats: heart healthy o Phospholipids: (Fig. 2.16b) Modified triglycerides Glycerol and 2 fatty acids+ a phosphorous containing group Heads are polar and tails are nonpolar Important in cell membrane structures o Steroids: (Fig. 2.16c) 4 interlocking ring structures Common steroids are cholesterol, vitamin D, bile salts, and steroid hormones Cholesterol is the most important:  Steroid synthesis  Bile salts synthesis  Building block of vitamin D  Hormones such as estrogen and testosterone  Required for cell plasma membrane structure o Eicosanoids: Derived from a fatty acid (arachidonic acid) Most important eicosanoids are Prostaglandins because they play a role in blood clotting, inflammation, labor contractions, and control of blood pressure Prostaglandins have 2 derivatives:  Prostacyclins  Thromboxanes  Proteins: ­ Comprise 20-30% of cell mass ­ Contain C, H, O, N, and sometimes S and P ­ Polymers of amino acid monomers are held together by peptide bonds ­ Have most varied functions of any molecules (structural, chemical, contraction) ­ Shape and function due to four structural levels ­ All proteins made up of 20 types of amino acids ­ Proteins contain an amine group and acid group (Fig. 2.2) ­ Can act as either base or acid . 4 structural levels of proteins: (Fig. 2.18a, b, c, d) 1. Primary: linear sequence of amino acids 2. Secondary: how primary amino acids interact with each other  Alpha helix coils resemble a spring  Beta pleated sheets resemble accordion ribbons 3. Tertiary : how secondary structures interact 4. Quaternary: how 2 or more different polypeptides interact with each other . Shapes of proteins fall into 2 categories: 1. Fibrous (structural) proteins: ­ Strand like, water insoluble, and stable ­ Most have tertiary or quaternary structure ­ Provide mechanical support ­ Ex. Keratin. Elastin. Collagen, and certain contractile fibers 2. Globular (functional) proteins: ­ Water soluble, compact, spherical, and sensitive ­ Specific functional regions such as active sites ­ Tertiary or quaternary structure ­ Ex. Antibodies, hormones, molecular chaperones, and enzymes . Denaturation: globular proteins unfold and lose their functional 3D shape ­ Active sites become deactivated ­ Can be caused by low pH or high temp. ­ Reversible if normal conditions restored ­ Irreversible if changes are extreme . Enzymes: globular proteins that act as biological catalysts ­ Speed up reactions and decrease activation energy needed to start a reaction ­ Act on specific substrates ­ Name usually ends in –ase . 3 steps in enzyme action: (Fig. 2.20) 1. Substrate binds to enzyme’s active site. Forming enzyme-substrate complex 2. Complex undergoes rearrangement of substrate resulting in final product 3. Product is released from enzyme  Nucleic acids: ­ Composed of C, H, O, N, and P ­ Largest molecules in the body ­ Made of monomers called nucleotides (composed of a nitrogenous bases, a pentose sugar, and a phosphate group) ­ 2 major groups: 1. Deoxyribonucleic acid (DNA) 2. Ribonucleic acid (RNA) ­ DNA holds the genetic info for the synthesis of all proteins (Fig. 2.21) ­ Nitrogenous bases: 1. Purines: Guanine (G) and Adenine (A) 2. Pyrimidines: Thymine (T) and Cytosine (C) ­ Complementary base pairing rules: A-T G-C ­ RNA: links DNA to protein synthesis and is single stranded Contains a ribose sugar Active mostly outside the nucleus Thymine (T) is replaced with Uracil (U) 3 types of RNA: 1. mRNA 2. tRNA 3. rRNA They all carry out the DNA orders for protein synthesis ATP: chemical energy released when glucose is broken down that directly powers chemical rxns in cells (Fig. 2.22) ­ Adenine containing RNA nucleotide with 22 additional phosphate groups ­ transports proteins, phosphorylates contractile proteins, and drives chemical rxns (Fig. 2.23) ­ loss of one phosphate group  ADP ­ loss of 2 phosphate groups  AMP Works Cited Lindsey, Jerri K., Katja Hoehn, and Elaine Nicpon Marieb. Human Anatomy & Physiology, 9th Edition Elaine N. Marieb, Katja Hoehn. Boston, MA: Pearson, 2013. Print.


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