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Biological molecules

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biological molecules . CARBOHYDRATES, FATS AND PROTEINS. includes how large molecules are made from smaller ones, their functions, etc. made in a very interactive way so that students can understand and clear all their concepts
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  • 1. CARBON OXYGEN HYDROGEN
  • 2.  Short term energy supply › Glucose produces ATP energy  Short term energy storage › Glycogen is stored in the liver and muscles  Structure › Plant cell walls, insect exoskeletons  Cell Membrane markers › Cell “identity tags”  All carbs have the formula Cn(H2O)n
  • 3. HYDROGEN + CARBON + OXYGEN = FATS =
  • 4.  Long term energy storage › Pack energy into a small space  Insulation and Padding › Protects organs  Structure › Cell membranes  Chemical Messengers › Steroids  All lipids do not dissolve in water = hydrophobic
  • 5. CARBON + OXYGEN + HYDROGEN + NITROGEN + SULPHUR
  • 6.  Starch is the nutrient storage form of carbohydrates in plants.  Glycogen is the nutrient storage form of carbohydrates in animal.  Cellulose is a rigid, structural carbohydrate found in the cells walls of many organisms.  Proteins are an extremely diverse group of biological molecules composed of the small molecules called amino acids.
  • 7.  Proteins are created by linking together amino acids into protein links called polypeptide chains. There are twenty amino acids of which 12 can be synthesized by the human body and 8 must be ingested in the foods we eat. These 8 are referred to as the essential amino acids.
  • 8.  Sequences of amino acids are strung together to produce polypeptide chains, which then fold up into working proteins.  Important groups of proteins include enzymes, which hasten chemical reactions, and structural proteins, which make up such structures as hair.  The primary structure of a protein is its amino acid sequence; this sequence determines a protein’s secondary structure—the form a protein assumes after having folded up  The activities of proteins are determined by their final folded shapes.  Antibodies help to fight diseases.
  • 9. ala ala gln gln ile ile . . . produces a polypeptide chain like this: A typical protein would consist of hundreds of amino acids The linkage of several amino acids . . .
  • 10. Figure 3.20 Primary structure Secondary structure Tertiary structure (a) (b) (c) (d) Quaternary structure amino acid sequence beta pleated sheet alpha helix random coil folded polypeptide chain two or more polypeptide chains Four Levels of Structure In Proteins The primary structure of any protein is simply its sequence of amino acids. This sequence determines everything else about the protein’s final shape. Structural motifs, such as the corkscrew-like alpha helix, beta pleated sheets, and the less organized “random coils” are parts of many polypeptide chains, forming their secondary structure. These motifs may persist through a set of larger-scale turns that make up the tertiary structure of the molecule Several polypeptide chains may be linked together in a given protein, in this case hemoglobin, with their configuration forming its quaternary structure.
  • 11.  There are about 20 different amino acids, each with a different chemical structure and characteristics; for instance, some are polar, others are non-polar. The final protein structure is dependent upon the amino acids that compose it. Protein function is directly related to the structure of that protein. A protein's specific shape determines its function.  antibodies and enzymes are proteins.
  • 12. Defensive proteins/anti bodies Virus Antibodies Bacterium Function: Protection against disease Example: Antibodies inactivate and help destroy viruses and bacteria.
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