Notes: Chapter 2.3 Carbon Compounds
Chemistry of Carbon 1.Carbon can form four covalent bonds. (tetravalence) 2.Carbon can bond with other carbon atoms, hydrogen, oxygen, nitrogen, phosphorus and sulfur. 6 protons 6 neutrons 6 electrons first shell- 2 second shell- 4
Single Bond A single bond is signified by a solid line between symbols; shares 2 electrons
Double Bond A double bond is signified by two solid lines between symbols; shares 4 electrons
Triple Bond A triple bond is signified by three solid lines between symbols; shares 6 electrons
Macromolecules 1.Macromolecules are “Giant molecules” 2.Consist of monomers (smaller units) that join together to form polymers (large molecules of repeating units – monomers- bonded together by covalent bonds. Macromolecules Macromolecules are “Giant molecules” Consist of monomers (smaller units) that join together to form polymers This process is called Polymerization.
Macromolecules The process of bonding monomers together is called polymerization Macromolecules Macromolecules are “Giant molecules” Consist of monomers (smaller units) that join together to form polymers This process is called Polymerization.
Dehydration Reaction Monomers are connected by a reaction in which 2 molecules are covalently bonded together through the loss of a water molecule.
Hydrolysis Breaking the covalent bond within the polymer to break off a monomer involves the breaking a water molecule and inserting its pieces.
Digestion When macromolecules are eaten, enzymes breakdown the polymers and released monomers are absorbed into the bloodstream.
Types of macromolecules 1.Carbohydrates 2.Lipids 3.Nucleic Acids 4.Proteins
Carbohydrates 1.Composition: made of C, H and O atoms 2.Monomer- monosaccharide 3.Polymer – polysaccharide 4.Uses: Main source of energy for organisms, structural purpose in cell membrane, and exoskeleton of insects.
Carbohydrates 4.Examples a.Sugars (Saccharides) 1.Monosaccharide = simple sugar molecule 2.Disaccharide = two monosaccharides bonded together with a glycosidic linkage
Glycosidic Linkage A covalent bond formed between 2 monosaccharide molecules by a dehydration reaction.
Carbohydrates b.Starches: Complex carbohydrates (polysaccharides) that store extra sugar 1.In animals, starch is called glycogen, structural is called chitin oChitin is used by arthropods to build their exoskeletons.
Carbohydrates 2. In plants, “plant starch”, structural is called cellulose oCellulose makes up the cell wall of plant cells. oHumans cannot breakdown cellulose during digestion. oKnown as “insoluble fiber”
Lipids 1.Composition: C, H, O and sometimes P atoms 2. Subunits: glycerol (“head”) and fatty acids (long carbon chain that makes up the “tail”) Glycerol Fatty Acid
Lipids 3. Not soluble in water – non-polar 4. Function: energy storage, main part of cell membrane, hormones, cushions vital organs and insulates the body 5. Examples: fats (3 fatty acid chains), phosopholipids (2 fatty acid chains), oils, waxes, steroids (hormones), cholesterol
Lipids 6. Types of fatty acids: a. Unsaturated fatty acids are found in lipids that are liquid at room temperature, C=C bonds The double bond creates a kink in the tails that keeps them from packing closely together. Example:Olive oil Double bond
Lipids b. Saturated fatty acids are found in lipids that are solids at room temperature, no C=C bonds Example:Shortening, butter
Saturated = only single bonds, maximum number of H atoms Unsaturated = at least on C = C double bond Types of Lipids lipid
Proteins 1.Composition: C, H, O, N 2.Function: 1.Structure 2.Storage 3.transport of other substances 4.movement 5.Immunity 6.Regulate Metabolism 7.Catalyze reactions (make them happen)
Proteins a)Made of monomers called amino acids that are linked together to form a chain 20 different types of amino acids All have the same general structure Draw this in your notes! Label!! Carboxyl Group
Some Amino Acids… General structureAlanineSerine Amino groupCarboxyl group
Warm- up 9/19 1.Monomers are joined together to form a polymer in what type of reaction? 2.How are a saturated and unsaturated fat structurally different? 3.What are 2 functions of a carbohydrate? Macromolecule s Quiz Tomorrow!!
4 Levels of Structure Primary a.Unique sequence of amino acids linked together to form a polypeptide chain –Changing the order of even 1 A.A. changes the shape and ability to function.
Secondary b.α- helix OR β- pleated sheet Repeatedly coiled or folded portions of the polypeptide chain as a result of hydrogen bonding at regular intervals along the backbone.
Tertiary c. 3D structure, interactions along different parts of the amino acid chain –This creates regions (hydrophobic, hydrophilic, etc) within the protein.
Quarternary Occurs when a protein consists of 2 or more polypeptide chains.
Nucleic Acids 1.Composition: C, H, O, N, P 2.Function: Store and transmit genetic information by determining the amino acid sequence in proteins 3.Two types a.DNA (deoxyribonucleic acid) b.RNA (ribonucleic acid)
Nucleotide 4.Made of monomers called nucleotides. A nucleotide has three parts a.5-carbon sugar (deoxyribose or ribose) b.Phosphate group c.Nitrogenous base (A, T, G, or C)
Carbon Compounds include that consist of which contain that consist of which contain CarbohydratesLipidsNucleic acidsProteins Sugars and starches Fats and oilsNucleotidesAmino Acids Carbon, hydrogen, oxygen Carbon, hydrogen, oxygen Carbon,hydrogen, oxygen, nitrogen, phosphorus Carbon, hydrogen,oxygen, nitrogen
Chapter 2.4: Chemical Reactions and Enzymes
Chemical Reactions Chemical Reaction: A change of one set of chemicals into another 1.Can be slow or fast 2.Chemical reactions require collisions between molecules which makes them unstable 3.Involves changes in chemical bonds AB + CD AC + BD
Chemical Reactions 1.Involves changes in chemical bonds a.Reactants are elements or compounds that enter into a chemical reaction. Bonds are broken in the reactants. b.Products are elements or compounds that result from a chemical reaction.
Chemical Reactions c. Whenever a reaction occurs that rearranges the atoms of molecules, bonds in the reactants must be broken and new bonds in the products must be formed.
Chemical Reactions 1.Involves changes in chemical bonds AB + CD AC + BD Which are the reactants? Which are the products? AB and CD AC andBD
Chemical Reaction Example: CO 2 in the body 1.Cells produce CO 2,then blood carries CO 2 from cells to lungs (exhale) Problem: CO 2 is not soluble (dissolvable) in water Solution: A chemical reaction converts CO 2 to a soluble compound
In blood, CO 2 converted to soluble compound: CO 2 + H 2 O → H 2 CO 3 In the lungs, reaction is reverse to exhale CO 2 H 2 CO 3 → CO 2 + H 2 O
Chemical reactions involve energy 1.Breaking and forming chemical bonds requires energy release or absorption 2.Reactions that release energy can occur spontaneously (but not all do) a.Energy is released as heat 3.Reactions that absorb energy will not occur without an energy source
4.What is activation energy? The energy needed to break the bonds in the reactants and get a reaction started. a.Some chemical reactions are really slow or require lots of energy and cannot occur on their own
Energy-Absorbing Reaction Energy-Releasing Reaction Products Activation energy Activation energy Reactants Endergonic/ Endothermic (Energy Inward) Exergonic/ Exothermic Energy Outward
Endergonic reaction – absorb free energy from the surroundings. Exergonic reaction – have a net release of free energy. –Can occur spontaneously.
Enzymes as catalysts 1.A catalyst - a substance that speeds up the rate of a chemical reaction by lowering the activation energy of the reaction. a.An enzyme is a protein that act as biological catalyst by speeding up reactions that take place in cells.
Enzymes as catalysts b. Enzymes provide a site (activation site) where reactants can be brought together to react. This decreases the activation energy and creates the “enzyme-substrate” complex.
Enzymes as catalysts c.Substrate- the reactants in a reaction involving an enzyme. a.The substrate must fit completely into the active site in order for the reaction to take place. d.Enzymes can be reused, but can only have one type of substrate a.If enough substrate is present, a single enzyme typically acts on 1,000 molecules per second.
Enzymes as catalysts e.The enzyme-substrate relationship is like that of a “lock and key” f.Enzymes can have an inhibitor in which another molecule can turn the enzyme on or off.
Inhibitors 1.Competitive inhibitors - Blocks the active site. 2.Non-competitive inhibitors - Bind to another part of the enzyme causing the shape of the active site to change making it useless.
Inhibitors 3.Allosteric inhibitors – Enzymes naturally go from active to inactive 1.An activator will bind causing the active form of a protein to remain stable. 2.An inhibitor will stabilize the inactive form of the enzyme.
More on Enzymes g. Denature – When enzymes lose their shape and functionality. This can be caused by: 1.pH 2.Temperature 3.Other proteins 4.Chemicals