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Biochemistry

Biochemistry. All Matter is composed of. Atoms. The Structure of the Atom ... Ions are atoms that have either a positive or negative electrical charge because ...

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Biochemistry

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    Slide 1:Biochemistry

    Slide 2:All Matter is composed of Atoms

    Slide 3:The Structure of the Atom

    Electrons: Negative electrical charge Protons: Positive electrical charge Neutrons: No net electrical charge

    Slide 4:Molecules

    Two or more atoms held together by Chemical bonds

    Slide 5:Chemical Bonds

    form because of the interactions between the electrons of the atoms

    Slide 6:The atom’s ELECTRONEGATIVITY (ability to attract electrons)

    Determines the type and strength of the Chemical bond

    Slide 7:Ions

    Ions are atoms that have either a positive or negative electrical charge because the electron number is NOT equal to the proton number

    Slide 8:IONIC BONDS

    Form between atoms when electrons are TRANSFERED from one atom to another forming ions of opposite electronic charges http://www.dac.neu.edu/physics/b.maheswaran/phy1121/data/ch09/anim/anim0904.htm

    Slide 9:Covalent Bonds

    Form when atoms share electrons Occur when the electronegativities between the atoms are similiar http://www.dac.neu.edu/physics/b.maheswaran/phy1121/data/ch09/anim/anim0904.htm

    Slide 10:Some molecules have Single Covalent Bonds… which means the atoms share one pair (a single pair) of electrons

    Slide 11:Some molecules have Double Covalent Bonds… which means the atoms share two pairs of electrons

    Slide 12:Some molecules have Triple Covalent Bonds… which means the atoms share Three pairs of electrons

    Slide 13:Nonpolar Covalent Bonds

    Occur when the electronegativities of both atoms are identical and the electrons are shared equally

    Slide 14:Polar Covalent Bonds

    Occur when the electronegativities of both atoms are Different and the electrons are shared unequally Negative Pole Positive Pole

    Slide 15:Hydrogen Bonds

    Hydrogen bonds are weak bonds which form between molecules Hydrogen Bond

    Slide 16:Bond Strengths

    Ionic Bonds are weak and are easily broken in water Covalent Bonds are generally strong Hydrogen Bonds are very weak

    Slide 17:The Properties of Water

    1. Water is the Universal Solvent. Ionic compounds and Polar covalent molecules readily dissolve in water

    Slide 18:Hydrophilic Molecules (water-loving)

    Are substances that dissolve in water…. Salts, sugars, etc….

    Slide 19:Hydrophobic Molecules (water-fearing)

    Are substances that do not dissolve in water… oils, waxes, etc…

    Slide 20:Water Has A High Specific Heat Capacity…. The capacity of a substance to change temperature in response to a gain or loss of heat… water changes temperatures very slowly

    Specific Heat - the amount of heat needed to raise 1 g of the substance 1 degree C. Why? ……… Hydrogen bonding.

    Slide 21:Water Has A High Heat Of Vaporization

    Heat of Vaporization: the quantity of heat a liquid must absorb for 1g of it to convert to a gaseous state.

    Slide 22:Liquid Water Is Cohesive

    Water sticks to water. Why? Because the polarity of water results in hydrogen bonding.

    Slide 23:Liquid Water is Adhesive

    Water sticks to other molecules. Why? Hydrogen bonding.

    Slide 24:Water transport in trees uses Cohesion and Adhesion

    Slide 25:Water Has A High Surface Tension

    The surface of water is difficult to stretch or break. Why? Hydrogen bonding.

    Slide 26:Water Stabilizes Temperature

    Water can absorb and store a huge amount of heat from the sun. Result - climate moderation Result - organisms are able to survive temperature changes.

    Evaporative Cooling

    Slide 28:Result:

    Water cools organisms from excessive heat buildup. Why? As water evaporates it takes the heat with it.

    Slide 29:Water Expands and becomes less dense when It Freezes….so it floats

    The distance between water molecules INCREASES from the liquid to the solid form. Why? Hydrogen bonding

    Water Benzene Floats Sinks

    Slide 31:Result

    Ice floats and forms an blanket of insulation during the winter……….Aquatic life can live under ice.

    Slide 32:Water is used to make Solutions

    A Solution is a Homogeneous mixture of two or more substances. Solvent + Solute Solution Sugar water, Saltwater, Pepsi

    Slide 33:Solvent

    The dissolving agent Present in a greater proportion Examples: Water Methane

    Slide 34:Solute

    The substance that is dissolved. Present in smaller quantity Examples: Salt in saltwater Sugar in sugar water

    Slide 35:Solution Concentration

    Usually based on Molarity Molarity - the number of moles of solute per liter of solution. A mole is = 6.021x1023

    Slide 36:One Mole of each

    Sulfur Sugar Copper Sulfate Mercury Oxide Copper Sodium Chloride

    Slide 37:Dissociation of Water

    Water can sometimes split into two ions. In pure water the concentration of each ion is 10-7 M

    Slide 38:Adding certain solutes disrupts the balance between the two ions. The two ions are very reactive and can drastically affect a cell.

    Slide 39:Acids

    Materials that can release H+ Example: HCl HCl H+ + Cl- Hydrochloric acid, vinegar, etc…

    Slide 40:Effects of Acid Rain

    Slide 41:Bases

    Materials that can absorb H+ Often reduce H+ by producing OH- Example: NaOH NaOH Na+ + OH- Drano, Soaps, etc…….

    Slide 42:pH Scale

    A logarithmic scale for showing H+ concentration in a solution. pH = - log [H+]

    Slide 43:pH Scale

    Acids: pH < 7 Neutral: pH 7 Bases: pH >7

    Slide 44:Acids: pH <7 etc. Bases: pH >7 etc. Each pH unit is a 10x change in H+

    Slide 45:Buffers

    Materials that have both acid and base properties. Resist pH shifts. Cells and other biological solutions often contain buffers to prevent damage.

    Slide 46:Organic Molecules

    Contain carbon atoms, exceptions are carbon monoxide and carbon dioxide Carbon has 4 electrons available to form 4 chemical bonds….therefore large molecules are easily formed using carbon as the backbone. Large carbon based molecules are usually found as long chains or rings.

    Slide 47:Macromolecules

    Most macromolecules are “polymers” ….molecules that consist of a single unit (monomer) repeated many times.

    Slide 48:Functional Groups

    Many organic molecules share similar properties because they have similar clusters of atoms, called the….. Function Groups Each Functional Group gives the molecules a particular property, such as acidity or polarity.

    Slide 49:Functional Groups

    Slide 50:Four Main Types Of Macromolecules

    Carbohydrates Lipids Protein Nucleic acids

    Slide 51:Carbohydrates

    Used for fuel, building materials, and receptors. Made of C,H,O General formula is CH2O C:O ratio is 1:1

    Slide 52:Types Of Carbohydrates

    Monosaccharides Disaccharides Polysaccharides

    Slide 53:Monosaccharides

    Mono - single Saccharide - sugar Simple sugars. Can be in linear or ring forms. Glucose, Fructose, Galactose…. all with the chemical formula C6H12O6….. Same chemical formula, different shapes.

    Slide 54:Most words ending with the letters OSE are carbohydrates. Glucose, Fructose, Galactose

    Slide 55:Disaccharides

    Sugar formed by joining two monosaccharides together thru the process of Dehydration Synthesis….(removing water)…aka…. Condensation Synthesis. all with the chemical formula C12H22O11 glucose + fructose = sucrose (table sugar) + H2O glucose + galactose = lactose ( the sugar in milk) + H2O glucose + glucose = maltose + H2O

    Slide 56:Condensation Synthesis or Dehydration Synthesis

    The chemical reaction that joins monomers into polymers. Covalent bonds are formed by the removal of a water molecule between the monomers.

    Slide 57:Hydrolysis

    Reverse of condensation synthesis. Using water (Hydro), to split (Lysis) Breaks polymers into monomers by adding water

    Slide 60:Examples of Disaccharides produced through Dehydration Synthesis

    Maltose = glucose + glucose Lactose = glucose + galactose Sucrose = glucose + fructose

    Slide 61:Polysaccharides all with the chemical formula (CH2O)n

    Many joined simple sugars. Used for storage or structure. Examples: Starch - a polymer of a-glucose molecules, principle energy storage molecules in plants Glycogen - a polymer of a-glucose molecules, principle energy storage molecules in animals, stored in the liver and muscles cells Cellulose - a polymer of b-glucose molecules, principle structural molecules in plant cell walls…. Major component of wood Chitin - a polymer of b-glucose molecules, each modified with a nitrogen group, principle structural molecule in the cell walls of fungi and the exoskeletons of the arthropods.

    Slide 64:Lipids (Fats)

    Diverse hydrophobic molecules which are insoluble in water (and other polar molecules) and soluble in non-polar molecules like ether and chloroform Made of C,H,O No general formula. C:O ratio is very high in C

    Slide 65:Types of Lipids (Fats)

    Triglycerides Phospholipids Steroids

    Slide 66: Triglycerides

    Three fatty acids joined to one glycerol. Joined by an “ester” linkage between the -COOH of the fatty acid and the -OH of the alcohol. Differ in which fatty acids are used. Used for energy storage, cushions for organs, insulation.

    Acid Fat

    Slide 68:Fats and Oils

    Fats - solid at room temperature. Oils - liquid at room temperature. Saturated - solid at room temperature. Unsaturated - liquid at room temperature.

    Slide 69:Saturated Fats

    Saturated - no double bonds.

    Slide 70:Unsaturated Fats

    Unsaturated - one or more C=C bonds. Can accept more Hydrogens. Double bonds cause “kinks” in the molecule’s shape.

    Slide 72:Question ?

    Which has more energy, a kg of fat or a kg of starch? …. (Hint) in Fats there are more C-H bonds which provide more energy per mass. Answer… carbohydrates (starch) have 4 calories per gram, lipids have 9 calories per gram

    Slide 73:Phospholipids

    Similar to fats, but have only two fatty acids. The third -OH of the glycerol is joined to a phosphate group replacing a fatty acid Major component of the Plasma Membrane of all cells

    Slide 74:Result

    Phospholipids are amphipathic which means they have a nonpolar, hydrophobic tail, but a polar, hydrophilic head. Self-assembles into bilayers, an important part of cell membranes.

    Slide 76:Steroids

    Characterized by a backbone of four fused carbon rings. Differ in the functional groups attached to the rings. Examples: cholesterol sex hormones

    Slide 77:Proteins

    Made of C,H,O,N, and sometimes S. No general formula Polymers of amino acids

    Slide 78:Uses Of Proteins

    Structural Proteins: used to make skin, hair, muscles, etc… Enzymes: Control Metabolism Antibodies: Provide protection against foreign substances Transport Proteins: Transport molecules across membranes Storage: such as ovalbumin in eggs

    Slide 79:Proteins

    Proteins are Polypeptide chains of Amino Acids linked by peptide bonds.

    Slide 80:Amino Acids

    All have a Carbon with four attachments: -COOH (acid) -NH2 (amine) -R group 20 different kinds of amino acids because there are 20 different kinds of R groups Amino Group Carboxyl Group AKA: Acid Group

    Slide 81:Amino Acids

    Slide 82:Amino Acids

    Slide 83:R groups

    The properties of the R groups determine the properties of the protein.

    Slide 84:Polypeptide Chains

    Formed by dehydration synthesis between the carboxyl group of one amino acid and the amino group of the second Amino Acid.

    Slide 86:Levels Of Protein Structure

    Organizing the polypeptide into its 3-D functional shape. Primary Secondary Tertiary Quaternary

    Slide 87:Primary Structure

    Order of amino acids in the polypeptide chain. Many different sequences are possible with 20 AAs.

    Slide 88:Secondary Structure

    3-D structure formed by hydrogen bonding between the R groups. Two main secondary structures: - a helix - pleated sheets

    Slide 89:Tertiary

    3D shape as bonding occurs between the R groups. Examples: Hydrophobic interactions Ionic bonding Disulfide bridges Hydrogen Bonding

    Slide 90:Quaternary

    When two or more polypeptides unite to form a functional protein. Example: hemoglobin

    Slide 91:Is Protein Structure Important?

    Slide 92:Denaturing Of A Protein

    Events that cause a protein to lose structure (and function). Example: pH shifts high salt concentrations heat

    Slide 94:Nucleic Acids

    Stores the genetic Information Polymers of nucleotides Made of C,H,O,N and P No general formula Examples: DNA and RNA

    Slide 95:Nucleotides of DNA and RNA

    Nucleotides have three parts: Nitrogenous Base Pentose sugar (Deoxyribose in DNA and Ribose in RNA) Phosphate Group

    Slide 96:Nitrogenous Bases

    Rings of C and N Two types: Pyrimidines (single ring) Thymine, Cytosine Purines (double rings) Adenine, Guanine

    Slide 97:Pentose Sugar

    5-C sugar Ribose - RNA Deoxyribose – DNA

    Slide 99:DNA: Deoxyribonucleic Acid

    Double Helix Structure The two strands of DNA are antiparallel, oriented in opposite directions… one strand is arranged in the 3’ – 5’ direction while the other is arranged in the 5’ – 3’ direction (5’ means the phosphate group is attached to the 5th carbon on the Deoxyribose molecule. Makes up genes.

    Slide 100:RNA: Ribonucleic Acid

    Important molecule in protein synthesis. Genetic information for a few viruses only.

    Slide 101:Differences between DNA and RNA

    RNA is a single strand DNA has Deoxyribose, RNA has ribose Thymine is replaced by Uracil

    Slide 102:Chemical Reactions in Metabolic Processes

    In order for chemical reactions to occur, the reacting molecules must first collide and then have enough energy (Activation energy) to trigger the formation of new bonds. Some reactions require catalysts. Catalysts are molecules which trigger or accelerate chemical reactions without being chemically altered themselves.

    Slide 103:Metabolism

    Chemical reactions which occur within living organisms are called Metabolic reactions….. Two types of Metabolic Reactions: *Anabolic Reactions: Build molecules and store energy *Catabolic Reactions: Breakdown Molecules and release energy

    Slide 104:Chemical Equilibrium

    The net direction of metabolic reactions, forward or reverse, is determined by the concentration of the reactants and the products.

    Slide 105:Enzymes: Globular proteins which catalyze metabolic reactions.

    Enzyme: Catalyzes the Reaction Substrate: molecule acted upon Products: Resulting molecules Enzyme + Substrate Enzyme – Substrate Complex Enzyme + Products Maltase + Maltose Maltase + Maltose Complex Maltase + glucose + glucose Active Site

    Slide 106:Enzymes

    Most Enzymes end with the letters - ASE Enzymes are substrate specific….. Examples: Maltase can only breakdown Maltose Sucrase can only breakdown Sucrose Amylase can only breakdown Amylose

    Slide 107:Enzymes

    The efficiency of Enzymes is affected by: pH shifts: pepsinogen is only activated when stomach acids lower the pH Heat: denatures enzymes

    Slide 108:Cofactors

    Are nonprotein molecules that assist enzymes… since they are nonproteins they are used up in the reactions. A holoenzyme is the union of a cofactor and enzyme. The enzyme is called an Apoenzyme when it’s part of a holoenzyme

    Slide 109:Inorganic Cofactors

    Are usually metals, like Iron (Fe+2), Magnesium (Mg+2)

    Slide 110:CoEnzymes

    Are organic molecules which aid in enzyme reactions……. Some vitamins are coenzymes. Since they are nonproteins they are also used up in the reactions.

    Slide 111:ATP Adenosine TriPhosphate

    Source of Activation energy for Metabolic Reactions

    Slide 112:Allosteric Enzymes

    Have two types of binding sites…. One for the substrate and one for the allosteric effector. Two types of Allosteric Effectors: 1. Allosteric Activator – binds to the enzyme and changes its shape to induces a reaction 2. Allosteric Inhibitor – binds to the enzyme and induces inactivity

    Slide 113:Allosteric Enzymes

    Slide 114:Competitive Inhibition

    Is when an enzyme mimic occupies the active site preventing a reaction.

    Slide 115:Noncompetitor Inhibitor

    Prevents enzyme reactions by binding to the substrate at locations other than the active or allosteric site.

    Slide 116:Cooperativity

    Occurs when an enzyme becomes receptive to additional substrate molecules after one substrate molecule attaches to an active site. Example: Hemoglobin…… its binding capacity to additional oxygen molecules increases after the first oxygen fills the active site.

    Slide 117:Cooperativity

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