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Chapters 2-5

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Know chemistry vocabulary (review packet) Difference between types of bonds and how many bonds elements form (CHNOPS) hydrogen (weak bonds between molecules) ionic (lose electron) covalent (share electrons) polar v. nonpolar molecules

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polar molecule...results in v shape know properties of water (cohesion, adhesion, surface tension) high heat capacity solid less dense than liquid (ice floats) know differences between solution, solute, solvent, aqueous solution; hydrophilic and hydrophobic Water is an excellent solvent. Ionic and polar substances dissolve easily in water nonpolar substances do not dissolve in water Acids, bases, pH and buffers **Think about all of these concepts in terms of living systems. How do all of these concepts allow a living organism to function? or cause an organism to not function successfully?

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Carbon is the most important element in living things. Carbon-based life forms Carbon has the ability to make 4 bonds...resulting in incredible versatility in bonding with other elements (it can make large, complex molecules) Hydrocarbons (carbon and hydrogen only)--fossil fuels Isomers (structural v. geometric) Structural- differ in covalent arrangement of atoms Geometric- differ in spatial arrangements Enantiomer- mirror images can form branches, chains and rings

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polymer--long molecule made of smaller building blocks carbohydrates, proteins, nucleic acids. **lipids** monomer--building blocks that make up polymers synthesis of polymers dehydration reactions--covalent bonds between molecules with the loss of a water molecule breakdown of polymers hydrolysis--molecules are broken using water (reverse of dehydration rxn) enzymes: macromolecules that speed up chemical reactions

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Functional Groups--chemical groups attached to carbon skeleton that determine function and unique properties of large molecules Figure 4.9 testosterone vs. estradiol

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Functional Groups Each has specific chemical properties, when attaches to larger molecule it gives those properties to that molecule A single molecule may contain many different functional groups Determines molecular shape and reactivity Hydroxyl (-OH) Alcohols Polar Hydrogen bond with water Carbs, proteins, nucleic acids and lipids

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Carbonyl (-CO) ketones and aldehydes Component of sugars Carbohydrates, nucleic acids Carboxyl (-COOH) important part of amino acids organic acids (ie. vinegar) Proteins, lipids Amino (-NH 2 ) important part of amino acids Basic (H+ acceptor) Proteins, nucleic acids

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Sulfhydryl (-SH) present in certain amino acids (methionine and cysteine) Forms disulfide bridge (protein structure) proteins Phosphate (-OPO 3 ) part of cellular energy sources (ATP, ADP) Acidic Nucleic acids Methyl (-CH 3 ) part of DNA molecules (gene expression) proteins

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Have the general formula C n H 2n O n Functions Source of stored energy Used to transport energy Structural molecules Used as building blocks for other macromolecules Recognition or signaling molecules that trigger specific responses

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Monosaccharide: simple sugar Pentose sugar (5 carbon) C 5 H 10 O 5 Ribose, deoxyribose Hexose sugar (6 carbon) C 6 H 12 O 6 Glucose**, fructose, galactose (isomers) Fructosefruit sugar, very sweet! Example of how arrangement of carbon atoms change molecule properties

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Polysaccharide: polymer of monosaccharides Formed by glycosidic linkages (covalent bond that results from dehydration reactionlose H 2 O) sugar bond Sucrose (glucose + fructose)disaccharide Used in carbohydrate transport Lactose (glucose + galactose)disaccharide Milk sugar Some individuals are missing the enzyme to break down this sugarlactose intolerance

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Starch (glucose+ glucose+ glucose.) Storage polysaccharide (plants) Molecules broken by hydrolysis for energy Long chain of alpha-glucose molecules Glycogen-- highly branched polymer of alpha-glucose Storage polysaccharide (animals) in liver and muscles animal starch Celluloseunbranched polymer of beta-glucose Structural polysaccharide (plant cell wall) Not easily broken down by most organisms Herbivores have special bacteria to do this Chitin (modified glucose chain) Structural material found in arthropods (insects) and fungi Makes up exoskeletons

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Group of molecules that are insoluble in water Hydrophobic May be storage fats, oils, steroids, or waxes Important component of cell membranes Phospholipids (phosphate attached to glycerol) 2 FA instead of 3 Polar and nonpolar ends of molecule (hydrophilic and hydrophobic regions) Phosphate hydrophilic Serve as a long-term form of energy storage Very efficient molecule for storage

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Made of two components: Fatty acid tail of molecule Long chain hydrocarbons with carboxyl group Chain is usually 14-20 carbons long Glycerol head of molecule Three OH groups (hydroxyl) alcohol Holds molecule together FA and glycerol held together by an ester linkage Carboxyl + Hydroxyl

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Triglyceride- one glycerol plus 3 FA (basic fat/oil) Saturated FA No double bonds (carbon atoms) Maximum number of hydrogens Solid at room temperature (animal fats-- butter) Unsaturated FA One or more double/triple bonds (carbon atoms) Liquid at room temperature (plant fats--oils) Monounsaturated (one double/triple bond) Polyunsaturated (more than one double/triple bond) trans fats partially hydrogenated unsaturated fats. Created by adding hydrogen and breaking double/triple bonds (health risks)

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Waxes Alcohol + unsaturated oil Steriods 4 carbon rings Attached functional groups make them unique (testosterone vs. estrogen) Ex. Cholesterol (component of cell membranes and precursor to other steriods)

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DNA and RNA Genetic information inherited from parents RNA used in protein synthesis Polymers of nucleotides Sugar, phosphate, nitrogenous base

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Every dynamic function of an organism depends on proteins! Functions include: (Fig. 5.15) Transport (hemoglobin) Structure (collagen) Enzymes (trypsin) Movement (myosin) Defensive (immunoglobin) Hormones (insulin) Storage (caesin)

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Proteins are made of monomers called amino acids. 20 amino acids exist in nature (fig. 5.16) Each has an amino and carboxyl group Chains of amino acids are called polypeptides Amino acids are linked together with a peptide bond Each polypeptide has an amino group at one end and a carboxyl group at the other The unique properties and structure are determined by the side groups of the amino acid (unique to each a.a.)

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A polypeptide chain becomes a protein once it has undergone modification and folding (3-dimensional) The 3-D structure is determined by the unique sequence of amino acids. (each protein is folded uniquely) Four Levels (fig. 5.20) Primarychain of a.a. (not folded) SecondaryH-bonds form between a.a. (making helix or pleated sheet) Tertiary 3-D shape formed from reactions between a.a. side chains (sulfide bridges) Quaternary multiple polypeptides (chains) linked together in 3-D structure

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Proteins exposed to excessive heat, pH changes, chemical, or other environmental changes may change their shape and become ineffective (misshapen)