the basics of chemistry for biology atoms: the units of elements bonding: covalent vs. ionic water:...

Download The Basics of Chemistry for Biology Atoms: The units of elements Bonding: Covalent vs. Ionic Water: Water‘s unique properties

If you can't read please download the document

Upload: eustace-garrison

Post on 26-Dec-2015

213 views

Category:

Documents


0 download

TRANSCRIPT

  • Slide 1
  • Slide 2
  • The Basics of Chemistry for Biology Atoms: The units of elements Bonding: Covalent vs. Ionic Water: Waters unique properties
  • Slide 3
  • The Chemistry of Life Matter (anything that takes up space) Composed of atoms Atom Smallest unit of an element that has the properties of the element 2 regions Nucleus Electron cloud
  • Slide 4
  • Inside the Atom: Subatomic Particles Protons: positive charged particles found in the nucleus (p + ) Neutrons: neutral particles found in the nucleus (n) Electrons: negative particles found in the electron cloud (e - ) Move around the nucleus in energy levels
  • Slide 5
  • Energy Levels of the Electron Cloud The number of electrons on each level is given by the formula 2n 2 where n is the level number Number/Name# of e - it can hold 1-K2 2-L8 3-M18 4-N32 5-O50 6-P72 7-Q98
  • Slide 6
  • Slide 7
  • Info from the Periodic Table Symbol Atomic Number (Z) = Number of p + Mass Number (A) = p + + n
  • Slide 8
  • Nuclides A Z X Copper Oxygen
  • Slide 9
  • Practice Set Symbol/Na me Atomic Number Atomic Mass NuclideProtonsNeutronsElectrons O Oxygen Au Gold Na Sodium K Potassium Cl Chlorine F Fluorine Ca Calcium
  • Slide 10
  • Lets Draw an Atom 1.Write the nuclide. 2.Draw the Energy levels. 3.Write the number of protons and neutrons in the nucleus. 4.Place the correct number of electrons on each energy level. 5.Leave unused energy levels empty.
  • Slide 11
  • Practice Drawing
  • Slide 12
  • Ions For a neutral atom, protons = electrons Ion: an atom with more or fewer electrons than it should normally have, causing a charge Loss of electrons forms a positive ion Cation Gain of electrons forms a negative ion Anion
  • Slide 13
  • Isotopes Isotopes: atoms of the same element with different masses due to different # of neutrons radioactive isotopes: unstable nuclei breakdown over time (nuclear decay)
  • Slide 14
  • Summary Chart Subatomic particle number to be changed How changedAtom is now a __ of the original atom Electron Gained Lost Anion (negative ion) Cation (positive ion) NeutronGained or LostIsotope
  • Slide 15
  • Bonding and Compounds Compound: two or more atoms bonded together due to electron exchange (give & take) or electron sharing
  • Slide 16
  • Metals Metals are found mainly in columns I to III They give away electrons to bond This forms positive ions: cations
  • Slide 17
  • Non-metals Non-metals are found mainly in columns III to VIII They can take in electrons from a metal to bond and form negative ions: anions They can share electrons with another non- metal and form molecules
  • Slide 18
  • Ionic Bonding Ionic Bonding: involves the giving of electrons by metals and the taking of electrons by non-metals Examples Sodium chloride Calcium chloride Sodium oxide Forms IONS
  • Slide 19
  • Ionic bonding
  • Slide 20
  • Covalent Bonding Covalent Bonding: the sharing of electrons between two non-metals Carbon dioxide Methane Nitrogen dioxide Diphosphorus pentoxide Forms MOLECULES
  • Slide 21
  • Covalent Bonding
  • Slide 22
  • Polarity Polar: electrons are not shared equally between the two non-metals in a covalent bond Non-polar: electrons are shared equally between the two non-metals in a covalent bond
  • Slide 23
  • Polar covalent bond
  • Slide 24
  • Polar/nonpolar bonds
  • Slide 25
  • van der Waals forces: forces of attraction between molecules Weak forces van der Waals forces
  • Slide 26
  • van der Waals interactions Weak interactions between molecules or parts of molecules that are brought about by localized change fluctuations Due to the fact that electrons are constantly in motion and at any given instant, ever-changing hot spots of negative or positive charge may develop
  • Slide 27
  • Hydrogen bonds Hydrogen atom covalently bonded to one atom is also attracted to another atom (oxygen or nitrogen) on another molecule Strong Water is best example
  • Slide 28
  • Cohesion Cohesion: attraction of molecules of the same substance to each other Example water molecules to other molecules in a glass
  • Slide 29
  • Waters Properties Polar~ opposite ends, opposite charges Cohesion~ H+ bonds holding molecules together (same substance, water to water) Adhesion~ H+ bonds holding molecules to another substance Surface tension~ measurement of the difficulty to break or stretch the surface of a liquid Specific heat~ amount of heat absorbed or lost to change temperature by 1 o C Heat of vaporization~ quantity of heat required to convert 1g from liquid to gas states Density.
  • Slide 30
  • Density Less dense as solid than liquid 1.Due to hydrogen bonding 2.Crystalline lattice keeps molecules at a distance
  • Slide 31
  • Mixtures Combination of 2 or more elements physically but not CHEMICALLY (not bonded together)
  • Slide 32
  • Wet Mixtures Soution zAll components are distributed evenly zParts 1.Solute: is dissolved 2.Solvent: does the dissolving Example: Kool-aid dissolved in water Suspension zComponents are distributed unevenly, just mixed together zParts 1.Supernant: liquid 2.Precipitate: solid Example: snowglobe
  • Slide 33
  • Acid/Base & pH Dissociation (breaking apart) of water into a hydrogen ion and a hydroxide ion Acid: increases the hydrogen concentration of a solution Base: reduces the hydrogen ion concentration of a solution pH: power of hydrogen Buffers: weak acids or bases that react with strong acids or bases to prevent changes in pH
  • Slide 34
  • pH Scale Acid Neutral Base 0 1 2 3 4 5 6 7 8 9 10 1112 13 14 Stronger WeakerWeakerStronger Human body prefers pH of 6.5 to 7.5
  • Slide 35
  • Acids vs. Bases Acid Acidic More H + than OH - Tastes sour Turns litmus paper red Found in coffee, tea, soft drinks, and fruit juices Base Alkaline More OH - than H + Tastes bitter Turns litmus paper blue Found in cleaners and soaps
  • Slide 36
  • Neutralization When Acids and Bases are mixed chemically, they produce salt and water. This reaction is called neutralization because the end products are not acidic nor alkaline, they are neutral!
  • Slide 37
  • 2006-2007 The Chemistry of Life What are living creatures made of? Why do we have to eat?
  • Slide 38
  • 96% of living organisms is made of: carbon (C) oxygen (O) hydrogen (H) nitrogen (N) Elements of Life
  • Slide 39
  • Molecules of Life Put C, H, O, N together in different ways to build living organisms What are bodies made of? carbohydrates sugars & starches proteins fats (lipids) nucleic acids DNA, RNA
  • Slide 40
  • Why do we eat? We eat to take in more of these chemicals Food for building materials to make more of us (cells) for growth for repair Food to make energy calories to make ATP ATP
  • Slide 41
  • What do we need to eat? Foods to give you more building blocks & more energy for building & running bodies carbohydrates proteins fats nucleic acids vitamins minerals, salts water
  • Slide 42
  • Water 65% of your body is H 2 O water is inorganic doesn t contain carbon Rest of you is made of carbon molecules organic molecules carbohydrates proteins fats nucleic acids Don t forget water
  • Slide 43
  • 2006-2007 How do we make these molecules? We build them! How do we make these molecules? We build them!
  • Slide 44
  • How to take large molecules apart Digestion taking big molecules apart getting raw materials for synthesis & growth making energy (ATP) for synthesis, growth & everyday functions + ATP
  • Slide 45
  • Example of digestion starchglucose ATP Starch is digested to glucose
  • Slide 46
  • Building large molecules of life Chain together smaller molecules building block molecules = monomers Big molecules built from little molecules polymers
  • Slide 47
  • Small molecules = building blocks Bond them together = polymers Building large organic molecules
  • Slide 48
  • Building important polymers sugar sugar sugar sugar sugar sugar nucleotide nucleotide nucleotide nucleotide Carbohydrates = built from sugars Proteins = built from amino acids Nucleic acids (DNA) = built from nucleotides amino acid amino acid amino acid amino acid amino acid amino acid
  • Slide 49
  • How to build large molecules Synthesis building bigger molecules from smaller molecules building cells & bodies repair growth reproduction + ATP
  • Slide 50
  • How to take large molecules apart Digestion taking big molecules apart getting raw materials for synthesis & growth making energy (ATP) for synthesis, growth & everyday functions + ATP
  • Slide 51
  • Example of digestion starchglucose ATP Starch is digested to glucose
  • Slide 52
  • Example of synthesis amino acidsprotein amino acids = building block protein = polymer Proteins are synthesized by bonding amino acids
  • Slide 53
  • Old Food Pyramid
  • Slide 54
  • New Food Pyramid
  • Slide 55
  • The Chemistry of Life
  • Slide 56
  • Carbon, the Backbone Carbon is special in the world of elements because it is able to bond to 4 other atoms at the same time!
  • Slide 57
  • Carbon, the Backbone Since Carbon can form so many bonds, it is considered the backbone of many compounds, that is Carbon is what the other atoms are all attached to
  • Slide 58
  • Special Covalent Bonds 1.Single bond: one pair of electrons is shared between two atoms 2.Double bond: two pair of electrons are shared between two atoms 3.Triple bond: three pair of electrons are shared between two atoms
  • Slide 59
  • Who can do these special cases? C, N, O, and S can all form double bonds. Only C and N can form triple bonds!
  • Slide 60
  • Carbons Shapes When Carbon bonds to other Carbon atoms, the resulting bond can take one of the following shapes: 1.Straight chain (in a straight line) 2.Branched chains (like the straight chain, but with a fork in the road 3.Ring structures
  • Slide 61
  • Carbohydrates Biochemical molecules that are used as both sources of energy and as short term energy storage commonly called sugars and starches
  • Slide 62
  • Glucose C 6 H 12 O 6
  • Slide 63
  • Carbohydrates, I Monosaccharides CH 2 O formula; simple sugars multiple hydroxyl (-OH) groups and 1 carbonyl (C=O) group: aldehyde (aldoses) ketone (ketoses) raw material for amino acids and fatty acids
  • Slide 64
  • Carbohydrates, II Disaccharides glycosidic linkage (covalent bond) between 2 monosaccharides; covalent bond by dehydration reaction Sucrose (table sugar) most common disaccharide
  • Slide 65
  • Carbohydrates, III Polysaccharides (Storage) Starch~ glucose monomers Plants: plastids Animals: glycogen Polysaccharides (Structural) Cellulose ~ most abundant organic compound; Chitin ~ exoskeletons; cell walls of fungi; surgical thread
  • Slide 66
  • Monomers and Polymers -mer: building blocks Monomer: one building block Polymer: many building blocks
  • Slide 67
  • Proteins Importance: instrumental in nearly everything organisms do; 50% dry weight of cells; most structurally sophisticated molecules known Monomer: amino acids (there are 20) ~ carboxyl (-COOH) group, amino group (NH 2 ), H atom, variable group (R). Variable group characteristics: polar (hydrophilic), nonpolar (hydrophobic), acid or base Three-dimensional shape (conformation) Polypeptides (dehydration reaction): peptide bonds~ covalent bond; carboxyl group to amino group (polar)
  • Slide 68
  • Primary Structure Conformation: Linear structure Molecular Biology: each type of protein has a unique primary structure of amino acids Ex: lysozyme Amino acid substitution: hemoglobin; sickle-cell anemia
  • Slide 69
  • Secondary Structure Conformation: coils & folds (hydrogen bonds) Alpha Helix:coiling; keratin Pleated Sheet: parallel; silk
  • Slide 70
  • Tertiary Structure Conformation: irregular contortions from R group bonding hydrophobic disulfide bridges hydrogen bonds ionic bonds
  • Slide 71
  • Quaternary Structure Conformation: 2 or more polypeptide chains aggregated into 1 macromolecule collagen (connective tissue) hemoglobin
  • Slide 72
  • Lipids No polymers; glycerol and fatty acid Fats, phospholipids, steroids Hydrophobic; H bonds in water exclude fats Carboxyl group = fatty acid Non-polar C-H bonds in fatty acid tails Ester linkage: 3 fatty acids to 1 glycerol (dehydration formation) Triacyglycerol (triglyceride) Saturated vs. unsaturated fats; single vs. double bonds
  • Slide 73
  • Lipids, II
  • Slide 74
  • Phospholipids 2 fatty acids instead of 3 (phosphate group) Tails hydrophobic (water fearing); heads hydrophilic (water loving) Micelle (phospholipid droplet in water) Bilayer (double layer); cell membranes
  • Slide 75
  • Steroids Lipids with 4 fused carbon rings Ex: cholesterol: cell membranes; precursor for other steroids (sex hormones); atherosclerosis
  • Slide 76
  • Nucleic Acids, I Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA) DNA->RNA->protein Polymers of nucleotides (polynucleotide): nitrogenous base pentose sugar phosphate group Nitrogenous bases: pyrimidines~cytosine, thymine, uracil purines~adenine, guanine
  • Slide 77
  • Nucleic Acids, II Pentoses: ribose (RNA) deoxyribose (DNA) nucleoside (base + sugar) Polynucleotide: phosphodiester linkages (covalent); phosphate + sugar
  • Slide 78
  • Slide 79
  • Nucleic Acids, III Inheritance based on DNA replication Double helix (Watson & Crick - 1953) H bonds~ between paired bases van der Waals~ between stacked bases A to T; C to G pairing Complementary
  • Slide 80
  • Give the complimentary DNA strand: AGTCTGCAAGTCTGCA
  • Slide 81
  • Give the complimentary RNA strand: AGTCTGCAAGTCTGCA
  • Slide 82
  • Biochemical Type CarbohydratesLipidsProteins Nucleic Acids MonomersMonosaccharides Sugars Fatty acids and glycerol Amino acidsnucleotides PolymersPolysaccharides Starches NONEPolypeptides, aka proteins polynucleotide Forces holding together Glycosidic linkagesEster linkages Peptide bondsBonds and van der Waals phosphodiester linkages UsesEnergy storage and structural support Energy storage, hormones, membranes Structural building materials Genetic information transfer
  • Slide 83
  • Biochemical Test CarbohydratesLipidsProteins Nucleic Acids Biuret's Reagent Blue turns violet in proteins, and pink with short-chain polypeptides proteins polypeptides Benedicts Solution Simple sugars heated with Benedicts turns from blue to red IodineStarches turn dark purple or black Brown Bag Test/ Sudan III stain Leaves spot on brown bag/ turns fats red
  • Slide 84
  • Conformation Test Lab
  • Slide 85
  • Lab Information In the laboratory investigation you will perform known tests using known reagents in order to obtain positive results for comparison with an unknown. Be sure to follow your lab directions exactly!
  • Slide 86
  • IDENTIFYING MACROMOLECULES IN FOOD LAB
  • Slide 87
  • Introduction Carbohydrates, proteins, and fats are all essential nutrients. We cannot manufacture these nutrients so we must obtain them from our environment.
  • Slide 88
  • Introduction In this lab, with the use of indicators as chemical detection tools, you will analyze a variety of foods for the presence of nutrients. Detection is based upon observing a chemical change that takes place most often a change in color.
  • Slide 89
  • Objective Identify the presence of major nutrients such as simple carbohydrates (glucose), complex carbohydrates (starch), protein and fat in common foods.
  • Slide 90
  • What is an indicator? Indicators are chemical compounds used to detect the presence of other compounds.
  • Slide 91
  • Background Information INDICATORMACRO- MOLECULE NEGATIVE TEST POSITIVE TEST Benedicts solution simple carbohydrate blueorange IKI solutioncomplex carbohydrate dark redblack Biuret solution proteinblueviolet, black Sudan IVlipiddark redreddish- orange
  • Slide 92
  • What is a Standard? An acknowledged measure of comparison for quantitative or qualitative value; a criterion.
  • Slide 93
  • Test for Simple Carbohydrates Benedict s solution Benedict's solution is a chemical indicator for simple sugars such as glucose: C 6 H 12 O 6. Aqua blue: negative test; yellow/green/brick red, etc.: positive test
  • Slide 94
  • Test for Simple Carbohydrates Benedict s solution Unlike some other indicators, Benedict s solution does not work at room temperature - it must be heated first.
  • Slide 95
  • Test for Complex Carbohydrates IKI solution IKI solution (Iodine Potassium Iodine) color change = blue to black
  • Slide 96
  • Test for Complex Carbohydrates IKI solution Iodine solution is an indicator for a molecule called starch. Starch is a huge molecule made up of hundreds of simple sugar molecules (such as glucose) connected to each other.
  • Slide 97
  • Test for Protein (amino acids) Biuret solution Biuret solution dark violet blue to pinkish purple
  • Slide 98
  • Test for Fats (lipids) Sudan IV Like lipids, the chemical Sudan IV is not soluble in water; it is, however, soluble in lipids. In this test dark red Sudan IV is added to a solution along with ethanol to dissolve any possible lipids.
  • Slide 99
  • Test for Fats (lipids) Sudan IV If lipids are present the Sudan IV will stain them reddish-orange (positive test).
  • Slide 100
  • Question Why didn t the test tube containing sucrose change colors?
  • Slide 101
  • Question Why didn t the test tube containing starch change colors?
  • Slide 102
  • Procedure Simple carbohydrate 1.Add 5ml distilled H 2 O using pipette to test tube 2.Add 1ml of food sample to test tube 3.Add 20 drops of Benedict solution 4.Place test tube in a hot water bath for 10 minutes.
  • Slide 103
  • Procedure Complex carbohydrate 1.Add 5ml distilled H 2 O using pipette to test tube 2.Add 1ml of food sample to test tube 3.Add 20 drops of IKI solution
  • Slide 104
  • Procedure Protein (amino acids) 1.Add 5ml distilled H 2 O using pipette to test tube 2.Add 1ml of food sample to test tube 3.Add 20 drops of Biuret solution
  • Slide 105
  • Procedure Fats (lipids) Add 5ml distilled H 2 O using pipette to test tube Add 1ml of food sample to test tube Add 20 drops of Sudan IV
  • Slide 106
  • LAB SAFETY and CLEAN UP WEAR safety goggles and apron at all times THOROUGHLY CLEAN lab area and equipment NO EDIBLE products in lab
  • Slide 107
  • Enzymes
  • Slide 108
  • Enzymes & Their Function
  • Slide 109
  • Reactions (Chemical Changes) Bonds are made or broken Energy is used or released Starting material: Reactant Ending material: Product
  • Slide 110
  • Enzymes Catalytic proteins: change the rate of reactions w/o being consumed Free E of activation (activation E): the E required to break bonds Substrate: enzyme reactant Active site: pocket or groove on enzyme that binds to substrate Induced fit model
  • Slide 111
  • Enzymes Learning objective: to examine what enzymes are and describe how they work.
  • Slide 112
  • Enzymes What are they? Why do we need them? Name some examples ?
  • Slide 113
  • Enzymes Globular proteins that catalyse chemical reactions in living organisms Properties
  • Slide 114
  • Enzymes Properties Specific
  • Slide 115
  • Enzymes Properties Specific Increase rate of the reaction
  • Slide 116
  • Enzymes Properties Specific Increase rate of the reaction Unchanged at the end of the reaction
  • Slide 117
  • Enzymes Globular proteins that catalyse chemical reactions in living organisms Properties Specific Increase rate of the reaction Unchanged at the end of the reaction Need them
  • Slide 118
  • Enzymes Globular proteins that catalyse chemical reactions in living organisms Properties Specific Increase rate of the reaction Unchanged at the end of the reaction Need them Reactions too slow to maintain life Cant increase temperatures/pressure in cells (fatal)
  • Slide 119
  • Enzymes Are Proteins The enzyme binds to the substrates by its active site The active site is a pocket formed by the folding of the protein where the substrates bind.
  • Slide 120
  • Enzymes Are Proteins The enzyme binds to the substrates by its active site The active site is a pocket formed by the folding of the protein where the substrates bind.
  • Slide 121
  • Active site The active site involves a small number of key residues that actually bind the substrates The rest of the protein structure is needed to maintain these residues in position
  • Slide 122
  • How do enzymes work?
  • Slide 123
  • An Example
  • Slide 124
  • Sucrose + H 2 O Glucose + Fructose
  • Slide 125
  • An Example Sucrose + H 2 O Glucose + Fructose Substrates Products
  • Slide 126
  • For a reaction to occur the sucrose and water would have to collide with enough energy to break and form bonds
  • Slide 127
  • For a reaction to occur the sucrose and water would have to collide with enough energy to break and form bonds This is the activation energy
  • Slide 128
  • Sucrose + H 2 OGlucose + Fructose + + SubstratesProducts
  • Slide 129
  • Energy Progress of reaction
  • Slide 130
  • Energy Progress of reaction Substrates
  • Slide 131
  • Energy Progress of reaction Substrates Products
  • Slide 132
  • Energy Progress of reaction Substrates Products High energy intermediate
  • Slide 133
  • Energy Progress of reaction Substrates Products High energy intermediate Activation energy
  • Slide 134
  • The minimum amount of energy needed to start the reaction, leading to the formation of a high energy intermediate = The Activation energy
  • Slide 135
  • Energy Progress of reaction Substrates Products High energy intermediate Activation energy Enzymes reduce the height of the energy barrier
  • Slide 136
  • Slide 137
  • Activation Energy In a natural reaction the product has a lower energy than the substrate so equilibrium will take it in the direction of the product. However there is an energy barrier to be overcome Enzymes lower the activation energy required to bring about a reaction. Ex. catalase reduces the activation energy for the reduction of H 2 0 2 86-fold
  • Slide 138
  • Enzyme Action What are the different models for enzyme action and which factors which control the rate of an enzyme reaction?
  • Slide 139
  • Lock and Key
  • Slide 140
  • However certain substances can bind to the enzyme at sites other than the Active site and modify its activity (inhibitors/co-factors) Idea that the enzyme is flexible
  • Slide 141
  • E S E S E PP
  • Slide 142
  • Induced Fit
  • Slide 143
  • How do enzymes work? Reaction Mechanism In any chemical reaction a substrate is converted into a product. In an enzyme catalysed reaction the substrate first binds to the active site of the enzyme to form the enzyme-substrate complex
  • Slide 144
  • Slide 145
  • Molecule Geometry Substrate molecule fits into the enzyme like a lock & key. Enzyme shape distorts or it changes other factors to make the reaction happen
  • Slide 146
  • Enzyme reactions enzyme + substrate enzyme-substrate complex
  • Slide 147
  • Enzyme reactions enzyme + substrateenzyme-substrate complex E +S ES Synthesis reaction since you are forming ONE product
  • Slide 148
  • Synthesis Reaction Active site es
  • Slide 149
  • Synthesis reaction Glucose-1-phosphate Starch
  • Slide 150
  • Enzyme reactions enzyme + product enzyme-substrate complex E +PES enzyme + substrateenzyme-substrate complex E +S ES Decomposition reaction since you are breaking down one thing into parts
  • Slide 151
  • Degradation reactions animation
  • Slide 152
  • Degradation reactions Starch Maltose
  • Slide 153
  • Catalase The enzyme catalase breaks down the waste substance hydrogen peroxide into water and oxygen. Hydrogen peroxide oxygen + water (enzyme) catalase (substrate) (products)
  • Slide 154
  • Degradation reaction SubstrateEnzymeProduct Hydrogen peroxide CatalaseOxygen and water StarchAmylaseMaltose MaltaseGlucose ProteinPepsinPeptides ProteaseAmino acids FatsLipaseFatty Acids and Glycerol
  • Slide 155
  • Enzyme activity How fast an enzyme is working Rate of Reaction
  • Slide 156
  • Enzyme activity How fast an enzyme is working Rate of Reaction Rate of Reaction = Amount of substrate changed (or amount product formed) in a given period of time.
  • Slide 157
  • Rate of Reaction Enzyme activity Variable you are looking at
  • Slide 158
  • Enzyme activity Four Variables
  • Slide 159
  • Enzyme activity Four Variables Temperature pH Enzyme Concentration Substrate Concentration
  • Slide 160
  • Effects on Enzyme Activity Temperature pH Cofactors: inorganic, nonprotein helpers; ex.: zinc, iron, copper Coenzymes: organic helpers; ex.: vitamins
  • Slide 161
  • Reaction rate factors Substrate concentration Initially rate increases with substrate concentration
  • Slide 162
  • Reaction rate factors Substrate concentration Initially rate increases with substrate concentration
  • Slide 163
  • Enzyme activity Temperature and pH affect the activity of an enzyme.
  • Slide 164
  • Rate of Reaction Temperature
  • Slide 165
  • Rate of Reaction Temperature 0203050104060
  • Slide 166
  • Rate of Reaction Temperature 0203050104060 40 o C - denatures 5- 40 o C Increase in Activity