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DO NOW Record and Answer these questions 1. What caused Kali’s brain infection? 2. Where did she contract her infection? 3. How many people survive this infection? http://www.youtube.com/watch?v=D2ggJhEKIi c DO NOW Gather with your Quicker Picker Upper Group You have 5min to refresh and prepare for presentation Hierarchy of Living Things Atom Molecule Cell Tissue Organ Organ System Organism Common Elements Element- made of only 1 type of atom 98% of all living things are made of… C H O N P S Connections of atoms that have unfilled outer rings Types of Bonds 1. Ionic *charged* Salts Metal + Nonmental ex. NaCl “table salt” 2. Hydrogen Bond Sharing of an Hydrogen (H) atom Polar (slight charge) Causes water’s unique traits ex. H2O Types of Bonds cont… 3. Covalent Shares Electrons Types of Covalent Bonds NonPolar (equal e- sharing) A. Single H-H (shares 1 e- pair) B. Double C = C (shares 2 e- pair) C. Triple N ≡ N (shares 3 e- pair) 2. Polar (unequal e- sharing) 1. What element on the periodic table has the highest Electronegativity (most reactive)? Electronegativity The pull of electrons towards nucleus 1. NONPOLAR- 2 atoms with similar Electroneg. No charge, shares e- equally 2. POLAR- unequal sharing of atoms Slightly charged Ex. H2O, O steals more of the ethan the H’s H O H Water’s Unique Traits 1. Cohesion (sticks to itself & others) 2. Universal Solvent 3. Resists Temperature Change 4. Liquid is denser(heavier) than solid http://www.youtube.com/watch?v=p S7Q4pNm1HM Do Now Without looking at your notes, fill in “CURL”Water’s Unique Properties Functional Groups- common molecular setups FUNCTIONAL GROUP STRUCTURE PURPOSE Hydroxyl -OH In Water & Alcohols Keto O II C In Carbohydrates Amino Phosphate N / \ H Apart of Amino Acids (make up proteins) H O II O -P – O I O When bonded to another Phosphate, release energy! Macromolecules Large molecules formed by many covalent bonds 4 Macromolecules: 1. Carbohydrate 2. Lipid 3. Protein 4. Nucleic Acid Composition of Living Things 30% Water 70% Macromolecules Formation of Macromolecules Condensation: -H2O Makes Molecules H2 O Hydrolysis • +H2O • Breaks Molecules H2 O H 2O Carbohydrate Ratio for Carbohydrate= 1C : 2 H : 1O Functions 1. Easily stored and released Energy 2. Structure (Cellulose-hard part of plants) Types of Carbohydrates 1. Monosaccharide (1-7C) • Ex. Ribose (sugar in DNA) 2. Disaccharide (12C) • Ex. Sucrose (table sugar) 3. Polysaccharide- many branches • Ex. Starch (plant energy storage) • Ex2. Glycogen (mammal energy storage) • Ex3. Cellulose (plant structure) Lipids Only made of C & H chains “Hydrophobic”- Insoluble in Water (due to nonpolar covalent bonds) FUNCTION: Longterm energy storage Structure- cell membrane & body surfaces Thermal insulation Lipid Structure Shaped as a Triglyceride Fatty Acid Fatty Acid “Tri” Glycerol Fatty Acid “glyce” Either Saturated or Unsaturated Fatty Acid Chains Types of Lipids 1. Saturated Fat Single bonds Fatty Acids are rigid/straight Solid at Room Temp. 2. Unsaturated Fat • • 1 or more Double Bonds Double Bond causes kink F.A. pack together poorly Liquid at Room Temp. 3. Phospholipid “amphiphatic”- 1 side hydrophilic 1 side hydrophobic • Apart of Cell Membrane (aka. Phospholipid Bilayer) Metabolism Sum of the total chemical reactions in a system Uses or provides Energy (E) Types of Energy: 1. Potential- stored energy (fat storage) 2. Kinetic – energy of movements (exercise) Types of Metabolism 1. Anabolic (Endothermic) Requires an Energy input Glucose + Fructose + ENERGY Sucrose 2. Catabolic (Exothermic) • Releases Energy • Usually makes heat Sucrose - Energy Glucose + Fructose Digestion: Catabolic + Anabolic Anabolic and Catabolic Reactions usually fuel ANABOLIC each other CATABOLIC Energy FOOD (Carb, Lipid, Proteins) FAT STORAGE BODY ACTIVITIES Energy Anabolism makes 1kg of human body, but it requires the catabolism of 10kg of food Laws of Thermodynamics 1st Law- Energy is not Created or Destroyed 2nd Law- Not all Energy is used (some is unusable) Nucleic Acids RNA & DNA Polymers Made up of many Monomers (single molecules) Ribose or Deoxyribose Sugar Phosphate MONOMERS Nitrogen Base NUCLEIC ACID (RNA & DNA) POLYMER Nitrogen Bases (nucleotides) 1. Pyrimidine- 1 ring Cytosine (C) Thymine (T) Uracil (U) *only in RNA* 2. Purine- Double Ring Adenine (A) Guanine (G) Types of Nucleotides 1. Oglionucleotides- “Primers”, regulate amount of RNA & DNA 2. Polynucleotides- in RNA & DNA Largest polymers in the world! DO NOW 1. List the Purine Nitrogen Bases 2. List the Pyrimidine Nitrogen Base 3. What are the 3 monomers of Nucleic Acids? 4. Which metabolism adds energy to the system? 5. Which metabolism uses energy in the system? RNA vs. DNA RNA DNA Nitrogen Bases: AU CG Nitrogen Bases: AT CG Bendy due to H-Bond Stiff 1 Strand 2 Strands attractions RNA Structure The shape depends on how the H-Bonds make the RNA fold 3’ Phosphate Phosphate 5’ Pyrimidine (C or U) Ribose Sugar Ribose Sugar Purine (A or G) Outside H want to bond to eachother DNA Functions Informational molecule Ex. CATC different meaning than CAAC GENE EXPRESSION 1. Can be Copied (Replicated) 2. Can be Turned into RNA (Transcripted) 3. That RNA can be turned into a Polypeptide, protein chain (Translation) 3’ DNA Structure Phosphate Phosphate Ribose Sugar Pyrimidine (C or T) Purine (A or G) Ribose Sugar Phosphate Phosphate Ribose Sugar 5’ 5’ Purine (A or G) Pyrimidine (C or T) Ribose Sugar 3’ Nitrogen Base Bonds Hydrogen Bond A–T A–U Polar Covalent Bond C - G Genetics GENES: portions of DNA that get turned into RNA and then PROTEINS GENOME: complete set of DNA in an organism (not all of it is used) Human Genome: 3Billion base pairs Chimpanzee shares 98% of human genome Ex. Keratin (hard part in hair/nails) is only translated in Skin Cells, not muscle cells Protein Function Protein functions vary the most Amino Acid •Enzymes •Messenger •Antibodies •Storage •Hormones •Structural Peptide bond MONOMERS •Genetics Polypeptide Chain Aka. Protein Amino Acid POLYMER Amino Acid 100’s occur in nature, but only 20 occur in the proteins of all organisms 1. Primary Structure Sequence of Amino Acids (AA) Letters represent AA’s 20100 possibilities for a small polypeptide EX: HKDEST 2. Secondary Structure Hydrogen Bonds & Hydrophillic/phobic areas cause twists and decide the structure A. Alpha Helix α (helices) B. Beta Helix β (pleated sheet) 3. Tertiary Structure 3D Overall shape When a protein denatures- it loses shape and therefore, loses its function 4. Quaternary Structure 2+ polypeptides combined Ex. Spiderweb proteins are so strong because numerous interlocking B helices Denaturing Because proteins are held together by weaker forces, they are easily destroyed DENATURE: destroys protein structure Can be irreversible Heat pH Too much polar or nonpolar