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Condensation and Hydrolysis

Condensation and Hydrolysis. Condensation Two molecules combine Hydrolysis A molecule splits into two smaller ones. Carbohydrates. Monosaccharides 6 Carbon sugars Glucose Fructose Galactose 5 Carbon sugars Deoxyribose Ribose. Carbohydrates. Oligosaccharides Disaccharides

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Condensation and Hydrolysis

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  1. Condensation and Hydrolysis Condensation Two molecules combine Hydrolysis A molecule splits into two smaller ones

  2. Carbohydrates • Monosaccharides • 6 Carbon sugars • Glucose • Fructose • Galactose • 5 Carbon sugars • Deoxyribose • Ribose

  3. Carbohydrates • Oligosaccharides • Disaccharides • Sucrose • Lactose • Maltose • Formed by condensation reactions

  4. Fatty Acids • Carbon backbone • Carboxyl group (- COOH) • Unsaturated • One or more double bonds in backbone • Saturated • All single bonds in backbone

  5. Triglycerides • Neutral fats • Three fatty acids and a glycerol • Condensation reaction • Body’s mostabundant lipid • Functions: • Energy reservoir • Insulation

  6. Structure of Amino Acids • Central carbon atom • An amino group • A carboxyl group • A hydrogen atom • One or more atoms “R Group”

  7. Structural Formulas for Some Amino Acids

  8. Peptide Bond Formation • A type of condensation reaction

  9. Levels of Protein Structure • Primary structure: The sequence of amino acids in a polypeptide chain. • Secondary structure: The polypeptide chains folds on itself to form a helix or a pleated sheet. • Tertiary structure: The helix and or pleated sheet fold on itself to form a globular structure • Quaternary structure: two are more tertiary structures binding together.

  10. Second Level of Protein Structure • Hydrogen bonds • Helical coiling • Sheet-like pattern

  11. Third Level of Protein Structure • Additional folding of secondary structure • R Group interactions • Hydrogen bonds • Disulfide bridges

  12. Fourth Level of Protein Structure • Two or more polypeptide chains joined by • Weak bonds (Hydrogen bonds) • Covalent bonds between sulfur atoms and R groups • Collagen • Keratin • Hemoglobin

  13. Structural Changes by Denaturation • Disruption of three-dimensional shape of protein • Changes in temperature and pH • Loss of function • Some proteins have organic compounds attached • Glycoproteins • Lipoproteins

  14. DNA Double stranded Hydrogen bonds between strands Twisted helically Four kinds of nucleotide monomers (A, T, C, G) Encodes protein-building instructions RNA Single stranded Four kinds of nucleotide monomers (A, U, C, G) Do not encode protein-building instructions Key players in the protein-building processes mRNA, tRNA, rRNA Two types of Nucleic acid

  15. Nucleic Acids - DNA and RNA • Building blocks • Four kinds of nucleotides • Differ only in component bases

  16. Single Strand of Nucleic Acid A series of covalently bonded nucleotides Nucleotides form together by condensation reactions

  17. DNA

  18. In Conclusion • Organic compounds have elements covalently bonded to carbon atoms • Living cells assemble organic compounds: lipids, carbohydrates, proteins, and nucleic acids • The building blocks are amino acids, nucleotides, simple monosaccharide sugars, and fatty acids • Complex carbohydrates are energy storage forms and structural materials

  19. In Conclusion • Lipids are used as energy storage and structural components • Proteins are made of amino acids. They form structural part of the body as well and enzymes. • Nucleic acids are the basis of inheritance and reproduction • developed by M. Roig

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