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Intro to Macro molecules Macromolecules
Carbon The element of LIFE! Found in all living organisms!  We are always looking for carbon based life forms Organic molecules: molecules that contain carbon C6H12O6, CO2, CH4 Some molecules are made of just CARBON and HYDROGEN…we call these HYDROCARBONS These are important in FUEL (aka GASOLINE!!) Many organic molecules, such as fats, have hydrocarbon components Hydrocarbons can undergo reactions that release a large amount of energy Inorganic molecules: molecules that do not contain carbon H2O, NH3, O2
LE 4-4 Hydrogen (valence = 1) Oxygen (valence = 2) Nitrogen (valence = 3) Carbon (valence = 4)
Structure of Carbon Structure Valence electrons: 4 How many bonds can carbon make with other atoms? 4: single, double, or triple…as long as it has 4 lines touching it This makes carbon a versatile atom…it can make long chains of carbons, branched carbon structures, even ring structures with itself
LE 4-5 Propane Ethane Length 2-methylpropane (commonly called isobutane) Butane Branching 1-Butene 2-Butene Double bonds Cyclohexane Benzene Rings
Some important words to know Molecule Group of covalently bonded atoms Macromolecule large molecules composed of thousands of covalently connected atoms Functional Groups Group of atoms within a molecule that interact in PREDICTABLE ways Polar, non-polar, acidic, basic, charged (+/-) Hydroxyl group Carbonyl group   Carboxyl group Amino group Sulfhydryl group Phosphate group
DNA (nucleotide) ATP Two REALLY Important Molecules with  Phosphate Groups
LE 4-10aa STRUCTURE (may be written HO—) Ethanol, the alcohol present in alcoholic beverages NAME OF COMPOUNDS FUNCTIONAL PROPERTIES Is polar as a result of the electronegative oxygen atom drawing electrons toward itself. Alcohols (their specific names usually end in -ol) Attracts water molecules, helping dissolve organic compounds such as sugars (see Figure 5.3).
LE 4-10ac EXAMPLE STRUCTURE Acetic acid, which gives vinegar its sour taste FUNCTIONAL PROPERTIES NAME OF COMPOUNDS Has acidic properties because it is a source of hydrogen ions. Carboxylic acids, or organic acids The covalent bond between oxygen and hydrogen is so polar that hydrogen ions (H+) tend to dissociate reversibly; for example, Acetic acid Acetate ion In cells, found in the ionic form, which is called a carboxylate group.
LE 4-10ba EXAMPLE STRUCTURE Glycine Because it also has a carboxyl group, glycine is both an amine and a carboxylic acid; compounds with both groups are called amino acids. FUNCTIONAL PROPERTIES NAME OF COMPOUNDS Acts as a base; can pick up a proton from the surrounding solution: Amine (nonionized) (ionized) Ionized, with a charge of 1+, under cellular conditions
LE 4-10bc EXAMPLE STRUCTURE Glycerol phosphate NAME OF COMPOUNDS FUNCTIONAL PROPERTIES Makes the molecule of which it is a part an anion (negatively charged ion). Organic phosphates Can transfer energy between       organic molecules.
What are macromolecules made of? ,[object Object]
Poly=many
Mono=one
Think of a beaded bracelet….
each bead is a MONOMER
The entire bracelet is a POLYMER
Large variety of polymers but there are less than 50 monomers…kinda like the alphabet…lots of words, only 26 letters
Polymerization: THE PROCESS OF MAKING A LARGER MOLECULE BY PUTTING TOGETHER SMALLER MOLECULES
Three of the four classes of life’s organic molecules are polymers:Carbohydrates Proteins Nucleic acids ***Lipids/fats are not polymers but they are still macromolecules
Brief Overview of  4 Macromolecules Carbohydrates Monomer: monosaccharaides and disaccharides Polymer: polysaccharides aka complex carbohydrates (Starches) Proteins Monomer: Amino acids Polymer: Polypeptide Chain (PROTEINS) NucleicAcids Monomer: Nucleotide Polymer: Nucleic Acids (DNA and RNA) Lipids, fats, oils and steroids Monomer: NONE Polymer: NONE
How Would You Describe  These People?
Making and Breaking Polymers Polymerization:making polymers Dehydration Reaction Dehydrate means water loss When a water molecule (H-OH) is released to join a monomer to another monomer Hydrolysis Hydro- water Lysis- to break down Def: to break apart or disassemble a polymer by adding water (H-OH)
LE 5-2 Short polymer Unlinked monomer Dehydration removes a water molecule, forming a new bond Longer polymer Dehydration reaction in the synthesis of a polymer Hydrolysis adds a water molecule, breaking a bond Hydrolysis of a polymer
Carbohydrates Monomer: Monosaccharide Polymer: Disaccharide or Polysaccharide Link between monomers is called: Glycosidic Linkage Formed by a dehydration reaction Always have Carbon, Hydrogen, and Oxygens CxH2xOx Common name: sugar End with suffix “-ose” Function: Energy/fuel, structure, storage GLUCOSE!!!!  What all cells need for energy
Carbs continued Monosaccharides Glucose fructose Disaccharides sucrose Polysaccharides Starch In plant cells; chain of glucose molecules coiled up like a phone cord Glycogen Excess sugar in animal cells is stored in this form; highly branched and more complex chain of glucose monomers Stored in muscle and liver cells When body needs energy, glycogen is broken down into glucose  Cellulose Found in plant cell walls; made of glucose monomer;  building material;  aka FIBER; humans do NOT have the enzyme to break this polysaccharide down Passes through digestive tract and keeps it healthy but NOT a nutrient Some animals (cows) have microorganisms that live in their digestive tract that help break down cellulose Carbs are hydrophilic because of hydroxl group (-OH) Dissolve in water making sugary solutions Large carbs (starches and cellulose) do not dissolve  Think about your towels and clothes, duh!
Proteins Monomer: amino acids 20 amino acids Amine (NH2) and carboxyl (COOH) groups attached to carbon Only thing different is side chain…R-group Polymer: polypeptide chains (proteins) Link between monomers is called: polypeptide bond  Made by a dehydration reaction  (between amine group of one aa and carboxyl group of another aa) STRUCTURE of A.A. Amino group on one end (-NH2) Carboxyl  group on one end (COOH) Hydrogen R-group/side chain (changes) Function of Proteins: structural support Storage Transport cellular communications Movement defense against foreign substances Proteins account for more than 50% of the dry mass of most cells
Protein Structure Primary structure 1’ Order of amino acids in a polypeptide chain Secondary structure 2’ Polypeptide chain folds because of interactions between amino acids HYDROGEN BONDING Tertiary Structure 3’ Gives proteins 3-D shape VERY IMPORTANT to function of protein Beta pleated sheets and alpha helices fold based on interactions between R-groups of a.a. Hydrogen bonds, polar/non-polar interactions, acid/base interactions, disulfide bonds,  van der Waals forces Quaternary Structure 4’ the association of the polypeptide chains some proteins contain more than one polypeptide chain Each polypeptide chain in the protein is called a subunit Two or more subunits come together for a specific function HEMOGLOBIN On Red blood cells Its shape allows RBCs to carry oxygen all around your body!
Denaturation Unraveling/unfolding of protein Why would this be a problem? When protein loses its 3-D shape and thus its specific function Caused by: Unfavorable changes in pH, temperature or other environmental condition Disrupts the interactions between side chains and causes loss of shape Examples: Frying an egg Straightening your hair

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Macromolecule intro

  • 1. Intro to Macro molecules Macromolecules
  • 2. Carbon The element of LIFE! Found in all living organisms! We are always looking for carbon based life forms Organic molecules: molecules that contain carbon C6H12O6, CO2, CH4 Some molecules are made of just CARBON and HYDROGEN…we call these HYDROCARBONS These are important in FUEL (aka GASOLINE!!) Many organic molecules, such as fats, have hydrocarbon components Hydrocarbons can undergo reactions that release a large amount of energy Inorganic molecules: molecules that do not contain carbon H2O, NH3, O2
  • 3. LE 4-4 Hydrogen (valence = 1) Oxygen (valence = 2) Nitrogen (valence = 3) Carbon (valence = 4)
  • 4. Structure of Carbon Structure Valence electrons: 4 How many bonds can carbon make with other atoms? 4: single, double, or triple…as long as it has 4 lines touching it This makes carbon a versatile atom…it can make long chains of carbons, branched carbon structures, even ring structures with itself
  • 5. LE 4-5 Propane Ethane Length 2-methylpropane (commonly called isobutane) Butane Branching 1-Butene 2-Butene Double bonds Cyclohexane Benzene Rings
  • 6. Some important words to know Molecule Group of covalently bonded atoms Macromolecule large molecules composed of thousands of covalently connected atoms Functional Groups Group of atoms within a molecule that interact in PREDICTABLE ways Polar, non-polar, acidic, basic, charged (+/-) Hydroxyl group Carbonyl group Carboxyl group Amino group Sulfhydryl group Phosphate group
  • 7. DNA (nucleotide) ATP Two REALLY Important Molecules with Phosphate Groups
  • 8.
  • 9.
  • 10. LE 4-10aa STRUCTURE (may be written HO—) Ethanol, the alcohol present in alcoholic beverages NAME OF COMPOUNDS FUNCTIONAL PROPERTIES Is polar as a result of the electronegative oxygen atom drawing electrons toward itself. Alcohols (their specific names usually end in -ol) Attracts water molecules, helping dissolve organic compounds such as sugars (see Figure 5.3).
  • 11. LE 4-10ac EXAMPLE STRUCTURE Acetic acid, which gives vinegar its sour taste FUNCTIONAL PROPERTIES NAME OF COMPOUNDS Has acidic properties because it is a source of hydrogen ions. Carboxylic acids, or organic acids The covalent bond between oxygen and hydrogen is so polar that hydrogen ions (H+) tend to dissociate reversibly; for example, Acetic acid Acetate ion In cells, found in the ionic form, which is called a carboxylate group.
  • 12. LE 4-10ba EXAMPLE STRUCTURE Glycine Because it also has a carboxyl group, glycine is both an amine and a carboxylic acid; compounds with both groups are called amino acids. FUNCTIONAL PROPERTIES NAME OF COMPOUNDS Acts as a base; can pick up a proton from the surrounding solution: Amine (nonionized) (ionized) Ionized, with a charge of 1+, under cellular conditions
  • 13. LE 4-10bc EXAMPLE STRUCTURE Glycerol phosphate NAME OF COMPOUNDS FUNCTIONAL PROPERTIES Makes the molecule of which it is a part an anion (negatively charged ion). Organic phosphates Can transfer energy between organic molecules.
  • 14.
  • 17. Think of a beaded bracelet….
  • 18. each bead is a MONOMER
  • 19. The entire bracelet is a POLYMER
  • 20. Large variety of polymers but there are less than 50 monomers…kinda like the alphabet…lots of words, only 26 letters
  • 21. Polymerization: THE PROCESS OF MAKING A LARGER MOLECULE BY PUTTING TOGETHER SMALLER MOLECULES
  • 22. Three of the four classes of life’s organic molecules are polymers:Carbohydrates Proteins Nucleic acids ***Lipids/fats are not polymers but they are still macromolecules
  • 23.
  • 24.
  • 25. Brief Overview of 4 Macromolecules Carbohydrates Monomer: monosaccharaides and disaccharides Polymer: polysaccharides aka complex carbohydrates (Starches) Proteins Monomer: Amino acids Polymer: Polypeptide Chain (PROTEINS) NucleicAcids Monomer: Nucleotide Polymer: Nucleic Acids (DNA and RNA) Lipids, fats, oils and steroids Monomer: NONE Polymer: NONE
  • 26. How Would You Describe These People?
  • 27. Making and Breaking Polymers Polymerization:making polymers Dehydration Reaction Dehydrate means water loss When a water molecule (H-OH) is released to join a monomer to another monomer Hydrolysis Hydro- water Lysis- to break down Def: to break apart or disassemble a polymer by adding water (H-OH)
  • 28. LE 5-2 Short polymer Unlinked monomer Dehydration removes a water molecule, forming a new bond Longer polymer Dehydration reaction in the synthesis of a polymer Hydrolysis adds a water molecule, breaking a bond Hydrolysis of a polymer
  • 29.
  • 30. Carbohydrates Monomer: Monosaccharide Polymer: Disaccharide or Polysaccharide Link between monomers is called: Glycosidic Linkage Formed by a dehydration reaction Always have Carbon, Hydrogen, and Oxygens CxH2xOx Common name: sugar End with suffix “-ose” Function: Energy/fuel, structure, storage GLUCOSE!!!! What all cells need for energy
  • 31. Carbs continued Monosaccharides Glucose fructose Disaccharides sucrose Polysaccharides Starch In plant cells; chain of glucose molecules coiled up like a phone cord Glycogen Excess sugar in animal cells is stored in this form; highly branched and more complex chain of glucose monomers Stored in muscle and liver cells When body needs energy, glycogen is broken down into glucose Cellulose Found in plant cell walls; made of glucose monomer; building material; aka FIBER; humans do NOT have the enzyme to break this polysaccharide down Passes through digestive tract and keeps it healthy but NOT a nutrient Some animals (cows) have microorganisms that live in their digestive tract that help break down cellulose Carbs are hydrophilic because of hydroxl group (-OH) Dissolve in water making sugary solutions Large carbs (starches and cellulose) do not dissolve Think about your towels and clothes, duh!
  • 32. Proteins Monomer: amino acids 20 amino acids Amine (NH2) and carboxyl (COOH) groups attached to carbon Only thing different is side chain…R-group Polymer: polypeptide chains (proteins) Link between monomers is called: polypeptide bond Made by a dehydration reaction (between amine group of one aa and carboxyl group of another aa) STRUCTURE of A.A. Amino group on one end (-NH2) Carboxyl group on one end (COOH) Hydrogen R-group/side chain (changes) Function of Proteins: structural support Storage Transport cellular communications Movement defense against foreign substances Proteins account for more than 50% of the dry mass of most cells
  • 33.
  • 34. Protein Structure Primary structure 1’ Order of amino acids in a polypeptide chain Secondary structure 2’ Polypeptide chain folds because of interactions between amino acids HYDROGEN BONDING Tertiary Structure 3’ Gives proteins 3-D shape VERY IMPORTANT to function of protein Beta pleated sheets and alpha helices fold based on interactions between R-groups of a.a. Hydrogen bonds, polar/non-polar interactions, acid/base interactions, disulfide bonds, van der Waals forces Quaternary Structure 4’ the association of the polypeptide chains some proteins contain more than one polypeptide chain Each polypeptide chain in the protein is called a subunit Two or more subunits come together for a specific function HEMOGLOBIN On Red blood cells Its shape allows RBCs to carry oxygen all around your body!
  • 35. Denaturation Unraveling/unfolding of protein Why would this be a problem? When protein loses its 3-D shape and thus its specific function Caused by: Unfavorable changes in pH, temperature or other environmental condition Disrupts the interactions between side chains and causes loss of shape Examples: Frying an egg Straightening your hair
  • 36.
  • 37.
  • 38. Fats/Lipids Made of mostly carbon and hydrogen…some oxygen Usually not soluble in water Not a polymer but is made of molecular units Glycerol + 3 Fatty Acids= FAT Linkage is called ESTER linkage Dehydration reaction Function Energy storage Insulation waterproofing
  • 39. Types of Fats Saturated Solid at room temperature Animal fats All the carbons in the fatty acid chains contain the MAXIMUM # of hydrogen atoms around each atom SATURATED with hydrogen Only single bonds in fatty acid chain Unsaturated/polyunsaturated fats Liquid at room temperature Plant oils, fish oils One or more double bonded carbon atoms in fatty acid chain, then it is unsaturated
  • 41. Steroids Chemical messengers Structure 4 fused carbon rings Ex. Cholesterol, testosterone, estradiol Function structural component of mammalian cell membranes resilience and fluidity of human membranes mobilized for the synthesis of steroid hormones protecting the human skin against external irritants and for holding water content Improvement of water balance in human skin Enhanced barrier function for stratum Inhibition of aging of skin Water retention for hair
  • 42. Nucleic Acids Monomer: Nucleotide Structure of a Nucleotide Made of a phosphate group, a sugar (ribose or deoxyribose), and nitrogenous base Polymer: Chain of nucleotides (nucleic acids) Deoxyribonucleic acid (DNA) Ribonucleic Acid (RNA) Function DNA genetic instructions used in the development and functioning of all known living organisms Instructions to make RNA and proteins long-term storage of information NITROGENOUS BASES: Pyrimidines: cytosine and thymine Purines: guanine and adenine A binds to T and G binds to C in the polymer DNA RNA messenger between DNA and the protein synthesis complexes known as ribosomes essential carrier molecule for amino acids to be used in protein synthesis Three types: mRNA, tRNA, rRNA NITROGENOUS BASES: Pyrimidines: cytosine and uracil Purines: guanine and adenine A binds to U and G binds to C in the polymer RNA