Introduction to Chemistry Matter: Anything that has mass and volume States of Matter Physical properties Properties that do not change the chemical nature of matter •Boiling point •Melting point •Freezing point •Color •Density Chemical Properties Properties that do change the chemical nature of matter Oxidation Rusting of iron = Iron Oxide (FeO2) pH Flammability Frying an egg Physical & Chemical Changes All Matter is composed of : Atoms The – Means “unable to be cut” smallest particle of an element that still has the characteristics of that element Elements Substances that can’t be broken down into simpler substances 96% of human mass is made up of C, H, O, N Periodic Table of The Elements Atoms are made up of smaller subatomic particles Protons: positively charged (Located in the nucleus) Neutrons: neutrally charged (Located in the nucleus) Electrons: negatively charged (Located around the nucleus) Discovered by James Chadwick in 1932 Discovered by Ernest Rutherford in 1919 Discovered by J.J. Thomson in 1897 Each atom has the same number of protons and electrons Electrons located farther away from the nucleus have more energy Electrons have less mass than protons. 1 proton= 1870 electrons Atomic number = number of protons Atomic mass = number of protons & neutrons Electron # = Proton # in Neutral elements 2 He 4.003 Atomic number: Atomic mass: # of Protons # of Electrons # of Neutrons Isotopes Neutron #’s change 1 Hydrogen: Deuterium: H 1 1 H 2 1 Tritium H 3 When elements combine to form substances with two or more atoms… Compounds are formed Mixtures When one or more atoms are physically combined but NOT chemically combined (Individual atoms retain their own properties) Easily separated by non-chemical means Solutions Solute – Substance dissolved Solvent – Dissolves substances (Water is the universal solvent) Colloids – light does not penetrate Suspensions Solubility of Solutions The amount of solute a solvent can dissolve Solubility affected by: Temperature Concentration Intramolecular Bonds Forces of attraction that hold atoms together within a molecule. Stronger than intermolecular bonds 2 types covalent ionic Ions Ions are charged particles. Atoms have either lost or gained one or more electrons Ionic bond Cation Anion Redox Reactions Important in ATP synthesis Oxidation is a loss of electrons Reduction is a gain of electrons Redox Reactions Covalent Bond Occurs when atoms SHARE electrons Special Note Diatomic molecule Molecules are only formed with covalent bonds Molecules A group of atoms held together by covalent bonds Water, hydrogen gas, oxygen, carbon dioxide Intermolecular Bonds Intermolecular bonds refers to the forces of attraction that hold molecules together Considerably weaker than intramolecular bonds 3 types of intermolecular bonds Hydrogen bonds Van der Waals forces Molecule-ion attractions Uneven distribution of electrons results in a polar molecule –– + H+ + + Figure 3.2 –– –– ++ Hydrogen bonds H + + – – Hydrogen Bond A bond formed in polar molecules Cohesion & Adhesion: Due to Hydrogen Bonding Cohesion – The ability of hydrogen bonds to attract like molecules Adhesion – The ability of hydrogen bonds to attract different types of molecules Why can these animals walk on water? Capillary Action is Due to Adhesion How does the crown get water? Van der Waals forces are weak attractive forces that hold non-polar molecules together molecule-ion attraction Hydration shell forms as water surrounds the dissolved ions H2O The molecule that supports all of life Molality vs Molarity Molality – the # of moles solute which can be dissolved in 1 kg of solvent Molarity – the # of moles solute which can be dissolved in 1 liter of solution Water Important biological properties Cohesion Adhesion High specific heat Heat of vaporization Solvent of life Insulation of bodies of water (floating ice) in winter Heat & Temperature Heat – measurement of the total amount of kinetic energy in matter Temperature – measurement of the average kinetic energy of molecules Measurement of heat calorie (cal) = amount of heat required to raise the temperature of 1 g of water by 1°C - or – the amount of heat that 1 g of water releases when cooled by 1°C Calorie (kcal) = 1000 cal = amount of heat required to raise the temp of 1 kg of water by 1°C Specific Heat The amount of heat that must be absorbed or lost for 1 g of that substance to change its temperature by 1°C Important because water does not change temperature quickly & large bodies of water can store much heat to warm the air. Specific Heat of Water Heat is absorbed when hydrogen bonds break Heat is released when hydrogen bonds form Evaporative Cooling Due to the high specific heat, when water evaporated it removes much heat from the system, thereby cooling the organism Latent Heat Latent Heat is the heat given up or absorbed by a substance as it changes state. It is called latent because it is not associated with a change in temperature Heat of Vaporization The quantity of heat a liquid must absorb for 1 g of it to be converted from the liquid to the gaseous state The hydrogen bonds in ice Are more “ordered” than in liquid water, making ice less dense Hydrogen bond Figure 3.5 Ice Liquid water Hydrogen bonds are stable Hydrogen bonds constantly break and re-form The different regions of the polar water molecule can interact with ionic compounds called solutes and dissolve them Negative oxygen regions of polar water molecules are attracted to sodium cations (Na+). Positive hydrogen regions of water molecules cling to chloride anions (Cl–). – Na+ + – – Na+ Cl– + Cl – – + + – Figure 3.6 – + + – – + + – – Acids & Bases Acids are formed by hydrogen cations Bases are formed by hydroxide anions Acids Donate protons (Hydrogen Ions) to water to form hydronium ions pH 0-6.99 Taste Sour Turn litmus paper red Strong acids completely dissociate to form ions Dissociation of Water – + H H H H Figure on p. 53 of water dissociating H H H Hydronium ion (H3O+) + H Hydroxide ion (OH–) Bases Donate hydroxide pH 7.01-14 Accept protons Taste bitter Feel slimy Turn litmus paper blue Strong bases completely dissociate to form ions pH pH Scale Buffers Compounds that tend to neutralize the pH of a solution by combining with either H+ ions or OH- ions to keep the solution neutral Chemical Reactions Synthesis (A+BC) Decomposition (CA+B) Single Replacement (AB+C AC+B) Double Replacement (AB+CDAC+BD) Reactants are to the left of the arrow (Elements reacting) Products are to the right of the arrow (Stuff made) Subscripts CANNOT be changed Coefficients can be changed to balance an equation) Chemical Reactions Endothermic rxn’s absorb heat Exothermic rxn’s give off heat Endergonic rxn’s absorb energy Exergonic rxn’s give off energy Organic Chemistry Organic molecules are any molecules that contain atoms from three elements: carbon, hydrogen, and oxygen. For example, glucose is organic, since its molecular formula is C6H12O6 Carbon dioxide (CO2) is inorganic since it does not contain hydrogen. Covalent bonds link carbon atoms together in long chains that form the skeletal framework for organic molecules. These carbon skeletons may vary in: • Length • Shape (straight chain, branched, ring) • Number and location of double bonds • Other elements covalently bonded to available sites All organic molecules have two parts: The carbon backbone & the functional group Tetravalence of carbon allows for complex arrangement of carbon compounds Carbon atoms can form single, double, or triple covalent bonds Name and Comments (a) Methane Molecular Structural Formula Formula Ball-andStick Model SpaceFilling Model H CH4 H C H H (b) Ethane H H C2H H C C H 6 (c) Ethene (ethylene) H H H C2H4 H C C H H Hydrocarbons –Are molecules consisting of only carbon and hydrogen –Hydrocarbon chains are hydrophobic because the C—C and C—H bonds are nonpolar Hydrocarbons Found in fossil fuels and makes up the “tails” of lipids Fat droplets (stained red) Figure 4.6 A, B (a) A fat molecule 100 µm (b) Mammalian adipose cells Functional Groups groups of atoms acting as a unit, that give organic molecules their physical properties,their chemical reactivity, & solubility in aqueous solutions. most possess electronegative atoms (N, P, O, S... EASILY ATTRACT PROTONS) key bonds are : ester (C-O-C) & amide (O=C-N-) are ionizable at physiological pH -NH2 AMINE= amino acid -C=Ox CARBONYL= -COOHx CARBOXYL= -OHx HYDROXYL = -PO4 PHOSPHORYL= -SH SULFHYDRYL= -CH3 METHYL= aldehyde/ketone acid alcohol organic phosphate disulfide hydrocarbon hydroxyl group Polar group; the bond between the oxygen and hydrogen is a polar covalent bond. Makes the molecule to which it is attached water soluble. Polar water molecules are attracted to the polar hydroxyl group which can form hydrogen bonds. Organic compounds with hydroxyl groups are called alcohols. Carbonyl Group Functional group that consists of a carbon atom doublebonded to oxygen (-C=O) Is a polar group. The oxygen can be involved in hydrogen bonding, and molecules with his functional group are water soluble. Is a functional group found in sugars. Aldehyde = carbonyl group on end carbon of chain Ketone =- carbonyl group attached to internal carbon Carbonyl Group Carboxyl group Carboxyl : -COOH Functional group that consists of a carbon atom which is both doublebonded to an oxygen and single-bonded to the oxygen of a hydroxyl group (-COOH). Is a polar group and water soluble. The covalent bond between oxygen and hydrogen is so polar, that the hydrogen reversibly dissociates as H+. This polarity results from the combined effect of the two electronegative oxygen atoms bonded to the same carbon. Since it donates protons, this group has acidic properties. Compounds with this functional group are called carboxylic acids. amino group Functional group that consists of a nitrogen atom bonded to two hydrogen atoms & to the carbon skeleton (—NH2). Is a polar group and soluble in water. Acts as a weak base. The unshared pair of electrons on the nitrogen can accept a proton, giving the amino group a +1 charge. Organic compounds with this function group are called amines. Sulfhydryl group Functional group which consists of an atom of sulfur bonded to an atom of hydrogen (—SH). Stabilize the structure of proteins. (Disulfide bridges of proteins) Organic compounds with this functional group are called thiols. Phosphate group Functional group which is the dissociated form of phosphoric acid (H3PO4). Loss of two protons by dissociation leaves the phosphate group with a negative charge. Has acid properties since it loses protons. Polar group and soluble in water. Organic phosphates are important in cellular energy storage and transfer methyl group methyl group (—CH3) Non-polar hydrophobic functional group Polymerization Organic compounds are formed by polymerization Large carbon compounds are built up from smaller simpler molecules called MONOMERS Monomers can bind to one another to form complex molecules known as POLYMERS Macromolecules are very large polymers Polymerization Building and Breaking Polymers Monomers link to form polymers through a chemical reaction called a CONDENSATION REACTION or Dehydration Synthesis Water is released during the formation of polymers The BREAKDOWN of some complex molecules, such as polymers, occurs through a process known as HYDROLYSIS Hydrolysis is the reversal of a condensation reaction Dehydration Synthesis Hydrolysis 4 Groups of Organic Compounds Found in Living Things Carbohydrates (C-H-O 1:2:1 ratio) Lipids (C-H-O) Proteins (C-H-O-N)…sometimes S Nucleic Acids (C-H-O-N-P) Carbohydrates MONOSACCHARIDES are simple sugars in a 1:2:1 ratio GLUCOSE GALACTOSE = sugar found in milk FRUCTOSE = fruit sugar Chemical composition (C6 H12 O6) Important Monosaccharides Glucose ISOMERS Isomers Are molecules with the same molecular formula but different structures and properties 3 types Structural Geometric Enantiomers Structural isomers Isomers that differ in the covalent arrangement of their atoms. • Number of possible isomers increases as the carbon skeleton size increases. • May also differ in the location of double bonds. Geometric isomers Isomers which share the same covalent partnerships, but differ in their spatial arrangements. Result from the fact that double bonds will not allow the atoms they join to rotate freely about the axis of the bonds. Subtle differences between isomers affects their biological activity. Cis – H on same side Trans – H on opposite sides Cis vs Trans Enantiomers (aka Chiral molecules) Isomers that are mirror images of each other. Can occur when four different atoms or groups of atoms are bonded to the same carbon (asymmetric carbon). There are two different spatial arrangements of the four groups around the asymmetric carbon. These arrangements are mirror images. Usually one form is biologically active and its mirror image is not. Enantiomers L isomer D isomer L & D are used to describe left & right isomers From the latin “Levo & dextro” Enantiomers cannot be superimposed on each other Structure determines function (L-Dopa works, D-Dopa doesn’t) Carbohydrates DISACCHARIDES consist of two single sugars(monosaccharides) linked together by glycosidic linkage (Dehydration synthesis) Lactose = Milk sugar Sucrose = Table sugar Carbohydrates Carbohydrates POLYSACCHARIDE is a carbohydrate made of long chains of sugars (3 or more monosaccharides) Starch - Plants convert excess sugars into starches for long-term storage (Alpha linkage) Glycogen -Animals store glucose in the form of polysaccharide glycogen in the liver and muscles to be used as quick energy Cellulose -a structural polysaccharide contained in the cell walls of plants (ß linkage) Chitin – a polysaccharide found in the cell walls of fungi and the exoskeletons of insects and arthropods Starch Glucose Lipids Lipids are large, NONPOLAR organic molecules that DO NOT dissolve in water Oils, fats, waxes, and steroids are lipid based Lipid molecules use less OXYGEN than carbohydrates to store energy efficiently Used in biological membranes and as chemical messengers Monomers – Fatty acids & Glycerol Lipids UNSATURATED FATS are a liquid at room temperature (OILS). Double bonds can have hydrogen added SATURATED FATS are solid at room temperature NO double bonds Saturated or Unsaturated Fatty Acids Stearic acid Oleic acid Liquid at room temp Solid at room temp Lipids - Saturated and unsaturated Triacylglycerol Phospholipids – Make up the cell membrane Hydrophilic vs Hydrophobic Hydrophilic = Water loving Hydrophobic = Water fearing Proteins Chemical composition C-H-O-N-S Proteins are made up of smaller monomers called AMINO ACIDS Amino Acids differ ONLY in the type of R group they carry Amino acids composed of 3 parts 1. Amino Group 2. Carboxylic group 3. R-group (Makes 20 different amino acids) Peptide Bonds – link amino acids 20 Amino Acids Proteins Each protein has a specific, and complex shape Different shapes allow proteins to perform different functions Two Amino Acids bond to form a DIPEPTIDE during a condensation reaction (2 Amino Acids form a covalent bond, called a PEPTIDE BOND) Amino Acids can bond to each other one at a time, forming a long chain called a POLYPEPTIDE. Proteins are composed of one or more polypeptides. Protein Conformation Primary Structure – sequence of amino acids Secondary structure – Folding and coiling due to H bond formation between carboxyl and amino groups of non-adjacent amino acid. R groups are NOT involved. Tertiary structure – disulfide bridges, ionic bonding, or h-bonding of R-groups Quaternary structure – 2+ amino acid chains R- group interactions, H bonds, ionic interactions Primary Structure Secondary Structure Tertiary Structure Quaternary Structure Chaperonins Amino Acids Amino acid structure: NH3 - C - COOH Amino acids differ due to the R group The structure of the R-group determines the chemical properties of the amino acid Amino Acids The polar uncharged amino acids are hydrophilic & can form h-bonds Serine Threonine Glutamine Asparagine Tyrosine Cysteine Amino Acids The nonpolar amino acids are hydrophobic and are usually found in the center of the protein. They also found in proteins which are associated with cell membranes. Glycine Alanine Valine Leucine Isoleucine Methionine Phenylalanine Tryptophan Proline Amino Acids The electrically charged amino acids have electrical properties that can change depending on the pH. Aspartic Acid Glutamic Acid Lysine Arginine Histidine Amino Acids The electrically charged amino acids (Aspartic Acid, Glutamic Acid, Lysine, Arginine, and Histidine) have electrical properties that can change depending on the pH. Cysteine can form covalent disulfide bonds Proline had a unique structure and causes kinks in the protein chain When two amino acids are joined together, the bond formed is called a ________. Denaturing of Protein Denaturing of Protein Transfer protein from aqueous solution to an organic solvent (chloroform) Any chemical that disrupts h-bonds, ionic bonds, & disulfide bridges Excessive heat Changes in pH Enzymes Act as CATALYSTS that can speed up some reactions by more than a billion times! Enzymes work by a physical fit (Lock and Key) between the enzyme molecule and its SUBSTRATE, the reactant being catalyzed. Enzymes reduces the activation energy for the chemical reaction to occur. After the reaction, the enzyme is released and is unchanged, so it can be used many times Enzyme names end in -ase Enzyme & Substrate fit like a lock & key (Shape specific) pH or temperature can change the active site shape on any enzyme Active site is where the reactants bind to the enzyme Activation Energy The energy require to start a reaction is called Activation Energy Nucleic Acids Nucleic Acids •RNA and DNA made of nucleic acids •C-H-O-N-P atoms •Polymers of nucleotides •Nucleotides consist of a 5-carbon sugar, a phosphate group, and a nitrogenous base. •Store and transmit genetic information Nucleic Acids