1 / 33

Biochemistry

Learn about the key concepts of biochemistry, including the difference between organic and inorganic molecules, the importance of carbon, and the role of carbohydrates, lipids, nucleic acids, proteins, and enzymes in living organisms.

tedg
Download Presentation

Biochemistry

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  1. Biochemistry To be used with Biochemistry Guided Notes

  2. Organic vs. Inorganic Molecules Contains Carbon (C), Hydrogen (H), and Oxygen (O) (Example: C6H12O6) Does not contain C, H, and O at same time (Example: H20) Carbon is the key element—the element of life Water: makes up 60 to 98% of living things—necessary for chemical activities and transport Carbon can bond with itself and form many times for bonds (single, double, triple and rings) Salts: help maintain water balance Example: Gatorade—electrolytes 4 Organic Molecules: Carbohydrates Lipids Nucleic Acids Proteins Acids and Bases: -pH Scale -Important for enzyme function

  3. Carbohydrates • Sugars and complex carbohydrates (starches) • Contain the carbon, hydrogen, and oxygen (the hydrogen is in a 2:1 ratio to oxygen) • End in -ose

  4. Monosaccharides • Simple sugars • All have the formula C6H12O6 • Have a single ring structure • Example: Glucose

  5. Disaccharides • Double sugars • All have the formula C12H22O11 • Example: sucrose (table sugar)

  6. Polysaccharides • Three or more simple sugar units • Examples: • Glycogen: animal starch stored in the liver and muscles • Cellulose: indigestible in humans: forms cell wall in plants • Starches: used as energy storage

  7. How are complex carbohydrates formed? • Dehydration synthesis: combining simple molecules to form a more complex one with the removal of water • Example: • monosaccharide + monosaccharide  disaccharide + water • C6H12O6 + C6H12O6 C12H22O11 + H2O • polysaccharides are formed from repeated dehydration synthesis

  8. Monosaccharide + Monosaccharide 

  9. Disaccharide + Water

  10. How are complex carbohydrates broken down? • Hydrolysis: the addition of water to a compound to split it into smaller subunits • also called chemical digestion • Example: • disaccharide + water  monosaccharide + monosaccharide • C12H22O11 + H2O  C6H12O6 + C6H12O6

  11. Lipids • Lipids (Fats): lipids chiefly function in energy storage, protection, and insulation • contain carbon, hydrogen, and oxygen but the H:O is not in a 2:1 ratio • Examples: fats, oils, waxes, steroids • Lipids tend to be large molecules

  12. Lipids • Lipids are formed from one glycerol molecule and 3 fatty acids • 3 fatty acids + glycerol lipid (fat)

  13. 4 Types of Lipids • Fats: from animals • Saturated: solid at room temperature • All single bonds in the fatty acid tail • Very difficult to break down

  14. 4 Types of Lipids 2. Oils: from plants • Unsaturated: liquid at room temperature • Presence of a double bond in the fatty acid tail • Ex. Vegetable oils

  15. Four Types of Lipids 3. Waxes: ear wax, bees wax 

  16. 4 Types of Lipids 4. Steroids: • One important molecule that is classified in this category is cholesterol • High levels could lead to heart disease

  17. Proteins • Proteins: contain the carbon, hydrogen, oxygen, and nitrogen • Made at the ribosomes • Composed of amino acid subunits

  18. Proteins • Major Protein Functions: • Growth and repair • Energy • Usually end with -in: • Example: Hemoglobin

  19. Making Proteins • Dehydration synthesis of a dipeptide • Dipeptide: formed from two amino acids • amino acid + amino acid  dipeptide + water

  20. Breaking down Proteins • Hydrolysis of a dipeptide • dipeptide + water  amino acid + amino acid

  21. Proteins • Polypeptide: composed of three or more amino acids • These are proteins • Examples: insulin, hemoglobin, and enzymes • There are a large number of different types of proteins: • The number, kind and sequence of amino acids lead to this large variety

  22. Nucleic Acids • Nucleic Acids: present in all cells • DNA: contains the genetic code of instructions through the synthesis of proteins • found in the chromosomes of the nucleus • RNA: directs protein synthesis • found in nucleus, ribosomes & cytoplasm

  23. Enzymes • Catalyst: inorganic or organic substance which speeds up the rate of a chemical reaction without entering the reaction itself • Examples: enzymes (organic) and heat (inorganic) • Enzymes: organic catalysts made of protein • most enzyme names end in –ase • enzymes lower the energy needed to start a chemical reaction (activation energy)

  24. How enzymes work • Enzyme forms a temporary association with a the substance it affects • These substances are known as substrates. • The association between enzyme and substrate is very specific—like a Lock and Key • This association is the enzyme-substrate complex • While the enzyme-substrate complex is formed, enzyme action takes place. • Upon completion of the reaction, the enzyme and product(s) separate • The enzyme is now able to be reused

  25. Enzyme-Substrate Complex

  26. Enzyme Terms • Active site: the pockets in an enzyme where substrate fits • Usually enzyme is larger than substrate • Substrate: molecules upon which an enzyme acts • All enzymes are proteins • Coenzyme: non-protein part attached to the main enzyme • Example: vitamins

  27. Proteins in action    enzyme substrate -------------> product Lock and Key Model

  28. Factors Limiting Enzyme Action • pH: pH of the environment affects enzyme activity • Example: pepsin works best in a pH of 2 in stomach Amylase works best in a pH of 6.8 in mouth--saliva

  29. Factors Limiting Enzyme Action • Temperature: as the temperature increases the rate of enzymes increases • Optimum Temperature: temperature at which an enzyme is most affective • Humans it is 37 degrees C or 98.6 degrees F • Dogs between 101 and 102 F

  30. When Temperatures Get Too High • Denature: • Change in their shape so the enzyme active site no longer fits with the substrate • Enzyme can't function • Above 45 C most enzymes are denatured • Why do we get a fever when we get sick?

  31. General Trend vs. Denaturing

  32. Factors Limiting Enzyme Action • Concentration of Enzyme and Substrate • With a fixed amount of enzyme and an excess of substrate molecules • the rate of reaction will increase to a point and then level off • Leveling off occurs because all of the enzyme is used up • Excess substrate has nothing to combine with • Add more enzyme reaction rate increases again

  33. Enzyme-Substrate Concentration

More Related