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Organic Chemistry

Organic Chemistry. The Chemistry of Carbon. A. Carbons Versatility. Tetravalent - can form four bonds with other elements May form double bonds and triple bonds. Bond with itself forming Chains of various lengths The chains may branch. May form rings.

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Organic Chemistry

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  1. Organic Chemistry The Chemistry of Carbon

  2. A. Carbons Versatility • Tetravalent - can form four bonds with other elements • May form double bonds and triple bonds. • Bond with itself forming Chains of various lengths • The chains may branch. • May form rings

  3. B. Characteristics of Organic Compound • Carbon backbones • Composed of single units called monomers • Monomers are joined in a condensation reactionthat usually occurs between the –OH groups of two monomers. H2O is removed linking the two monomers with an oxygen bridge • Polymers- many joined monomers • Polymers are broken down in Hydrolysis

  4. II. 4 Major Classes of Organic Compounds

  5. A. Carbohydrates

  6. 1. Functions of Carbohydrates • Quick energy- sugar, glycogen and starch • Structure- cellulose, chitin

  7. 2. Structure of Carbohydrate • Glucose(C6H12O6) and Fructose (C6H12O6) are single sugars called monosaccharides • Isomers- compounds with the same molecular formula but different structures

  8. C) Disaccharide- two monosaccharides joined in a condensation reaction. An example is sucrose. • D) Polysaccharides- long chains of sugars • 1) Starch- storage form of carbohydrates in plants (1-4ά) • 2) Glycogen- storage form of carbohydrate in animals (1-4ά) • 3) Cellulose- structural polysaccharide in plants (1-4β)

  9. B. Lipids Animal Fat Plant Oils Waxes

  10. 1. Functions • Long term energy storage • Structure- form membranes • Insulation

  11. 2. Structure- 1 glycerol with fatty acid chains

  12. 3. Types of Lipids a) Saturated fat- each carbon is bonded with two hydrogens in the fatty acid chain • Animal fats • Solid at room temperature • Bad for you. (Cause arteriosclerosis)

  13. b) Unsaturated Fat- contains double bond between some of the carbons • Plant oils • Liquid at room temperature • Better for you. More easily absorbed

  14. c. Phospholipid- forms the membrane around cells

  15. C. Proteins

  16. 1 Functions: • Structure Example: collegen • Transport Example: hemoglobin • Fight Disease Example: antibodies • Communication Ex: Hormones • Movement Ex: actin and myosin • Control Chemical Reactions Example: enzymes

  17. 2. Structure- Shaped to perform function • Proteins are made of monomers called amino acids b) Amino acid structure: R group Amino group Acid group c) All amino acids have the same amino and acid groups but different r groups d) Peptide bonds join amino acids in condensation reactions forming a dipeptide

  18. Amino Acids with Hydrophobic Side Groups Note the methyl groups at the bottom of the chains

  19. Amino Acids with Hydrophilic Side Groups Note the charged or polar groups at the bottom of the chains

  20. And Some Amino Acids are in Between Hydrophobic and Hydrophilic regions influence protein shape.

  21. 3. Levels of Protein Structure • 1st Level: Linear sequence of amino acids • 2nd Level: Spiraling and pleating • 3rd Level: Bending and folding • 4th Level: Intertwining of multiple polypeptides

  22. 4. Proteins are able to function because of their complex shape 5. Enzymes Function (Enzymes control chemical reactions) E + S  E/S  E + P Enzyme-substrate complex Enzyme Substrate Enzyme Product a) Enzymes are specific to a substrate (like a lock and key) • Enzymes are named by adding “ase” to the name of the substrate

  23. The Catalytic Cycle of Enzymes Enzyme with empty active sites Hydrolysis occurs Substrate (Sucrose) Substrate is converted to product and the enzyme is not used up. The enzyme’s active sites are free to accept another substrate molecule Substrate binds with the enzyme forming an enzyme-substrate complex

  24. The Catalytic Cycle of Enzymes a) The enzyme binds with the substrate at the active site. Induced fit stresses key bonds b) The substrate is converted to product

  25. Factors Affecting Enzyme Activity 1. Substrate Concentration Adding more substrate will have no affect on the rate of the reaction passed the SATURATION POINT RATE Low CONCENTRATION High

  26. 2. Temperature Human enzymes have an optimal temperature of 37º Celsius. Higher temperatures cause the enzymes to denature. 37oC RATE 0 10 20 30 40 50 50 70oC

  27. 3. pH Most enzymes have an optimal pH of 7. Some enzymes function more effectively in acidic or basic conditions. RATE 1 2 3 4 5 6 7 8 9 10 11 12 13 14

  28. Nucleic Acids

  29. D. Nucleic Acids- large complex molecules formed of smaller smaller units called nucleotides 1. Nucleic acid structure • Nucleotide consists of a sugar, a phosphate group and a nitrogen base • Sugars: 1) Ribose in RNA 2) Deoxyribose in DNA C) Bases: 1) Purines (2 rings) Adenine & Guanine 2) Pyrimidines (1 ring) cytosine & Thymine

  30. Nucleic Acids • DNA structure is a double helixwith the base pairing of Thymine with Adenine and Cytosine with Guanine. • RNA structure is a single spiral with Uracil replacing Thymine. RNA Carries the genetic code from the nucleus to the ribosome.

  31. 4. Nucleic Acid Functions • DNA and RNA carry the genetic code. I.e. The information for constructing proteins • Other related nucleotides like Adenosine Triphosphate (ATP) supplies energy to the cell • Many other nucleotides and dinucleotides are involved in electron transport. • GTP, UTP, CTP • dGTP, dATP, dCTP, dTTP • AMP, NAD+, NADP, FAD

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