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Chemistry of Life Keri Muma Biology 6 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Matter • Matter is anything that occupies space and has mass • Matter is composed of chemical elements – Elements are substances that cannot be broken down into other substances Periodic Table Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings • Twenty-five elements are essential to life – Four of these make up about 96% of the weight of the human body – Trace elements occur in smaller amounts Figure 2.3 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings The Structure of Atoms • Each element consists of one kind of atom – An atom is the smallest unit of matter that still retains the properties Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Electron Arrangement • Maximum number of electrons per shell – 2 in the first shell; 8 in the other shells • Number of electrons on the outer shell – determines the atoms chemical behavior and the bonds it will form Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Ionic Bonds • When an atom loses or gains electrons, it becomes electrically charged – Ions are charged atoms – Ionic bonds are formed between oppositely charged ions Cation Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Anion Electrolytes – conduct electric currents • Some very important ions in humans: • Calcium (Ca 2+ ) – muscle contraction, blood clotting, bones • Sodium (Na+) – nerve impulses, muscle contraction, water balance • Potassium (K+) – nerve impulses and muscle contraction Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Covalent Bonds • Covalent bonds form when electrons are shared between atoms. Non-polar Polar Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Hydrogen bonds • The polarity of water results in weak attractions between neighboring water molecules – These interactions are called hydrogen bonds () () () Hydrogen bond () () () () () (b) Figure 2.11b Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Vital Properties of Water • High heat capacity – Requires a lot of energy to increase in temperature, and releases a lot of energy when it cools – Important in maintaining a constant body temperature • High heat of vaporization – As water evaporates it takes large amounts of heat with it – Good cooling mechanism Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Vital Properties of Water Solvent properties – Dissolves chemicals, making it a good medium for transporting biological molecules • A solution is a liquid consisting of two or more substances evenly mixed – Solvent: is the dissolving agent Ion in solution Salt crystal – Solute: is the substance being dissolved Figure 2.16 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Water is a Good Solvent • Hydrophilic – water soluble (likes water) – Polar molecules • Hydrophobic – does not dissolve in water (water fearing) – Non – polar molecules • Amphiphilic – molecules that is both hydrophilic and phobic Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Vital Properties of Water • Chemical reactivity – Hydrolysis – water breaks bond apart – Dehydration – removing water to form bonds Dehydration • Cohesion • Cushioning Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Hydrolysis Acids, Bases, and pH • Acid – A chemical compound that donates H+ ions to solutions HCl H+ + Cl- • Base – A compound that accepts H+ ions and removes them from solution NaOH Na+ + OH- Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Concept of pH • Measures concentration of hydrogen ions • Logarithmic scale – each pH unit is a tenfold change in H+ concentration – pH 7 = neutral – pH below 7 = acidic – pH above 7 = basic Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Concept of pH • Buffers are substances that resist pH change – They accept H+ ions when they are in excess – They donate H+ ions when they are depleted Bicarbonate ions as a buffer: CO2 + H2O H2CO3 HCO3- + H+ Figure 2.18 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings ORGANIC MOLECULES • A cell is mostly water but the rest of the cell consists mostly of organic molecules – Organic molecules are large molecules containing carbon (macromolecules) Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings ORGANIC MOLECULES • Each type of organic molecule has a unique threedimensional shape that defines its function in an organism – The molecules of your body recognize one another based on their shapes Receptor molecule Transmitting cell Receiving cell Signal molecule Figure 3.5 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings BIOLOGICAL MOLECULES • There are four categories of macromolecules in cells – Carbohydrates – Lipids – Proteins – Nucleic acids Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings • Most macromolecules are polymers – Polymers are made by stringing together many smaller molecules called monomers – Cells link monomers together to produce polymers – Organisms also have to break down macromolecules Short polymer Monomer Longer polymer (a) Dehydration synthesis of a polymer Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings (b) Hydrolysis of a polymer • Carbohydrates – Includes sugars and starches – Contain carbon, hydrogen, and oxygen (1:2:1 ratio) •Glucose C6H12O6 •Ribose C5H10O5 – Function: quick source of energy, biological markers Fructose Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Carbohydrates – Classified according to size • Monosaccharides – one sugar, referred to as simple sugars Examples: glucose, fructose Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Disaccharides • A disaccharide is a double sugar – It is constructed from two monosaccharides joined together Examples: maltose, sucrose Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Polysaccharides • Polysaccharides are complex carbohydrates formed by long chains of monosaccharides – Starch, cellulose (plants), glycogen (animals) Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Lipids – Carbon and hydrogen outnumber oxygen C57H110O6 – Lipids are hydrophobic – Functions: • Energy storage • Cushioning • Insulation Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Lipids • Neutral fats – mostly triglycerides – A combination of glycerol and three fatty acids – Found in fat deposits (adipose tissue) – Source of stored energy and insulation – Cushions organs Glycerol Fatty acid (a) Dehydration synthesis linking a fatty acid to glycerol Figure 3.15a Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings • Unsaturated fatty acids - have less than the maximum number of hydrogens bonded to the carbons – Examples: Most plant oils; vegetable or corn oil • Saturated fatty acids - have the maximum number of hydrogens bonded to the carbons – Example: Most animal fats What is a trans fat then??? Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Lipids • Phospholipids – Forms cell membranes and the myelin sheaths of neurons – Phosphate head (hydrophilic) and lipid tail (hydrophobic) Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Lipids • Eicosanoids – A 20 carbon fatty acid with a 5 or 6 carbon ring – Regulators of various physiological functions – Examples: prostaglandins, leukotrienes, thromboxanes Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Lipids • Steroids are very different from other fats in structure and function – The carbon skeleton is bent to form four fused rings • Cholesterol is the “base steroid” from which your body produces other steroids – Example: testosterone, estrogen, cortisol, bile salts Cholesterol Figure 3.16 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Proteins • A protein is a polymer constructed from chains of amino acid monomers • Contains C, H, O, N, and sometimes S • There are 20 different amino acids Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Amino Acids • The arrangement of amino acids makes each protein different • Amino acids are held together by peptide bonds • Humans have an estimated 2 million different proteins, 1 million have been identified as of 2007 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Types of Proteins • Fibrous proteins – Provides for construction materials for body tissues – Important role in structure – Examples: collagen, elastic fibers, myosin and actin Structural proteins Contractile proteins Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Types of Proteins • Globular Proteins – Complex folded structure – Plays a vital role in cell function – Act as enzymes, hormones, transport proteins or antibodies Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Protein Shape 5 1 • Primary structure – The specific sequence of amino acids in a protein 15 10 30 35 20 25 45 40 50 55 65 60 70 – Genetically determined 85 80 75 95 90 100 110 105 115 120 125 129 Figure 3.21 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Amino acid Protein Shape • Secondary structure -polypeptide folded into a helix or a sheet • Tertiary structure- sheets and helices folded into a 3-D globule • Quaternary structure - several tertiary units put together Figure 3.23 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Protein Shape • A slight change in the primary structure of a protein affects its ability to function – The substitution of one amino acid for another in hemoglobin causes sickle-cell anemia 1 2 (b) Sickled red blood cell Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings 6 7. . . 146 4 5 Normal hemoglobin (a) Normal red blood cell 1 3 2 3 6 7. . . 146 4 5 Sickle-cell hemoglobin Figure 3.22 What Determines Protein Structure? • A protein’s shape is sensitive to the surrounding environment – Unfavorable temperature and pH changes can cause a protein to unravel and lose its shape – This is called denaturation Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Nucleic Acids • Nucleic acids are information storage molecules – They provide the directions for building proteins – Two types: DNA and RNA Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Nucleic Acids • Nucleotides are the monomers of nucleic acids Each nucleotide consists of a: 5 carbon sugar Phosphate group Nucleic base Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Deoxyribonucleic acid • DNA is composed of 4 types of nucleotides • Purines – Adenine (A) Thymine (T) Cytosine (C) – Guanine (G) • Pyrimidines – Thymine (T) – Cytosine (C) Figure 3.25 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Deoxyribonucleic Acid (DNA) • Organized by complimentary base pairing to form a double stranded helix • The nucleotides of the two stands are joined by hydrogen bonds –A=T –G=C • Contains a sugar-phosphate backbone Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Ribonucleic acid • RNA is different from DNA in that: Nitrogenous base (A,G,C, or U) – Its sugar is ribose – It has the base uracil (U) instead of thymine (T) – It’s single stranded Uracil (U) Phosphate group Sugar (ribose) Figure 3.27 Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Nucleotides • Some other nucleotides are used to transfer and store energy or are used in chemical signaling – ATP used for cellular work – NAD and FAD, used as electron carriers in cellular respiration – GTP, cyclic AMP, ADP Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings Summary Copyright © 2004 Pearson Education, Inc. publishing as Benjamin Cummings