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Understanding Organic Molecules in Biochemistry

Dive into the world of organic molecules - carbohydrates, lipids, proteins, and nucleic acids - their structures, functions, and interactions in living organisms. Learn about hydrophilic and hydrophobic properties, functional groups, and macromolecular structures. Explore the significance of lipids, proteins, and nucleic acids, their building blocks, levels of structure, and denaturation processes. Unravel the secrets of DNA, RNA, and ATP in biological systems through antiparallel pairing and codons.

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Understanding Organic Molecules in Biochemistry

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  1. Chapter 4 - Organic Chemistry, Biochemistry Organic molecules are molecules that contain carbon and hydrogen. All living things contain these organic molecules: carbohydrates, lipids,proteins,andnucleic acids. These molecules are often called macromoleculesbecause they may be very large, containing thousands of carbon and hydrogen atoms and because they are typically composed of many smaller molecules bonded together.

  2. Carbon and Hydrogen

  3. Cont’d

  4. Hydrophilic and Hydrophobic • Polar and ionic molecules have positive and negative charges and are therefore attracted to water molecules because water molecules are also polar. They are said to be hydrophilic because they interact with (dissolve in) water by forming hydrogen bonds. Nonpolar molecules are hydrophobic. Polar and ionic molecules are hydrophilic

  5. Functional Groups • Organic molecules may have functional groups attached. A functional group is a group of atoms of a particular arrangement that gives the entire molecule certain characteristics. Functional groups are named according to the composition of the group.

  6. Condensation and Hydrolysis  Sucrose • This is called a condensation or dehydration synthesis reaction. • Energy is required to form a bond. • Hydrolysis • This is a type of reaction in which a macromolecule is broken down into smaller molecules. • It is the reverse of condensation (above).

  7. Macromolecules and Monomers • Example of a Macromolecule Monomer polysaccharide (complex carbohydrate) monosaccharide (simple sugar) fat (a lipid) glycerol + fatty acid protein amino acid nucleic acid nucleotide

  8. Monosaccharides Example: Glucose, fructose, and galactose are monosaccharides; their structural formula is C6H12O6.

  9. Disaccharides Sucrose (table sugar) is composed of glucose and fructose Lactose is found in milk and contains glucose and galactose. Polysaccharides Monosaccharides may be bonded together to form long chains called polysaccharides.

  10. Starch and Glycogenplant and animal storage respectively Cellulose and Chitin structural and functional

  11. Lipids • Lipids are compounds that are insoluble in water but soluble in nonpolar solvents.  • Some lipids function in long-term energy storage. Animal fat is a lipid that has six times more energy per gram than carbohydrates. • Lipids are also an important component of cell membranes.

  12. Fats and Oils (Triglycerides)

  13. Saturated and Unsaturated Fat

  14. Phospholipids Phospholipid Bilayer

  15. Steroids Cholesterol (see diagram above) is the precursor of several other steroids, including several hormones.   It is also an important component of cell membranes.

  16. Proteins Some important functions of proteins are listed below. • enzymes (chemical reactions) • hormones • storage (egg whites of birds, reptiles; seeds) • transport (hemoglobin) • contractile (muscle) • protective (antibodies) • membrane proteins (receptors, membrane transport, antigens) • structural • toxins (botulism, diphtheria)

  17. Amino Acids • Amino acids are the building blocks of proteins. • Twenty of the amino acids are used to make protein. Each has a carboxyl group (COOH) and an amino group (NH2).

  18. Polypeptides

  19. Levels of structure • Primary Structure • Secondary structure • Tertiary structure • Quaternary structure

  20. Denaturation • Denaturation occurs when the normal bonding patterns are disturbed causing the shape of the protein to change.  This can be caused by changes in temperature, pH, or salt concentration. For example, acid causes milk to curdle and heat (cooking) causes egg whites to coagulate because the proteins within them denature. •  If the protein is not severely denatured, it may regain its normal structure.

  21. Nucleic acids • DNA Antiparallel

  22. Complimentary base pairing • The adenine of one strand is always hydrogen-bonded to a thymine on the other. Similarly, Guanine is always paired with Cytosine. • A-T • G-C

  23. RNA

  24. Codons

  25. ATP

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