Unit 1(8): Digestion

  1. Acidic pH level and chemical balance
    • pH < 7 
    • Hydroxide < Hydrogen
  2. Which molecule is the primary energy source for cells?
    ATP
  3. Polymers and 2 examples
    • Multiple monomers that come together to form large chemical compounds.
    • Ex. Carbs and Proteins
  4. Catabolic
    • Large chemicals broken into smaller ones
    • Cata - to break
  5. The two types of metabolic reactions
    • Catabolic
    • Anabolic
  6. Which molecule is a combination of a carbohydrate and 2 inorganic molecules?
    Glucose (C₆H₁₂O₆)
  7. Types of carbohydrates and their descriptions
    • Monosaccharides - 1 sugar unit
    • Disaccharides - 2 sugar units
    • Polysaccharides - many sugar units (form rings)
  8. Examples of monosaccharides
    • Glucose
    • Galactose
    • Fructose
  9. Monomer
    A single molecule that can react with other monomers
  10. Disaccharide makeup and creation process
    Two monosaccharides put together by dehydration synthesis
  11. What are isomers? Give an example.
    • Isomers are chemicals that have the same chemical formula but a different arrangement of molecules
    • Glucose and fructose
  12. Metabolism
    All the chemical reactions in cells
  13. Basic (alkaline) pH level and chemical balance
    • pH > 7
    • Hydroxide > Hydrogen
  14. Neutral pH and chemical balance
    • pH ~ 7
    • Hydroxide = Hydrogen ions
  15. Polysaccharide definition and different storage types for plants and animals
    • Many monosaccharides put together
    • Plant storage: Starch
    • Plant structure: Cellulose
    • Animal storage: Glycogen
  16. What is the difference between glycogen, starch, and cellulose?
    The extent of cross branching causing different properties
  17. Functions of lipids
    • Structural materials - cell membranes, cushion for delicate organs, carriers for fat soluble vitamins
    • Energy reservoirs - excess glycogen in animals is converted into fat
  18. The 4 lipid groups
    • Triglycerides (fats/oils)
    • Phospholipids (membranes)
    • Waxes
    • Sterols (cholesterol/steroids)
  19. Triglycerides
    Union of 3 fatty acids with glycerol
  20. Animal triglycerides
    • Fats
    • Saturated (stable)
    • Single bonds (covalent)
    • Difficult for our bodies to digest
  21. Plant triglycerides
    • Oils
    • Poly unsaturated
    • Some double bonds 
    • Easier for our bodies to break down
  22. Phospholipids
    • 2 fatty acids and a phosphate group
    • Fat tail (hydrophobic)
    • Phosphate heads hydrophilic - good for cell membranes as its semi-permeable
  23. Steroids lipid group and hormone group
    • Sterols
    • Androgen - male sex hormones
    • Estrogen - female sex hormones
  24. Liposome
    • Double layered sphere used to: 
    •     - Carry drugs through the body that would otherwise be
    •        rejected
    •     - Gene-therapy to introduce new DNA to cells
  25. Problem with lipids
    Fats contain double the amount of energy as an equivalent mass of carbohydrates of proteins
  26. LDL (low-density lipoprotein)
    Bad cholesterol that clogs arteries
  27. HDL (high-density lipoprotein)
    Good cholesterol that carries LDLs to the liver to be broken down
  28. Formation of proteins
    • Polypeptides
    • Formed from 8 - 1000 amino acids joined to the acid group by peptide (covalent) bonds by dehydration synthesis
  29. What all is composed of proteins?
    • Ribosomes
    • Mitochondria
    • Muscles, nerves, skin, hair (mostly protein)
    • Antibodies and enzymes (specialized proteins)
  30. Dehydration synthesis
    Forms peptide (covalent) bonds; makes proteins
  31. Hydrolysis reaction
    Splits protein to make amino acids
  32. The body can not produce these (obtained in diets)
    Essential amino acids
  33. Primary Structure
    Linear (order of amino acids)
  34. What is molecular biology and give example
    • Each type of protein has a unique primary structure chain of amino acids
    • Ex. Iysozyme
  35. Secondary protein structure and what it's caused by
    • Coiled or folded 
    • Difference because of hydrogen bonds
  36. What is the coiled protein shape called?
    Alpha Helix
  37. What is the folded protein shape called?
    Beta-pleated sheet
  38. Tertiary protein
    Irregular contortions from R group bonding
  39. Quaternary protein
    2 or more polypeptide structures aggregated into 1 macromolecule
  40. What three things can change a protein's shape/function?
    • 1) Excess heat
    • 2) Radiation
    • 3) pH change
  41. Denaturation
    • Temporary change of a protein's shape/function
    • Might resume shape after factor is removed
  42. Coagulation
    Permanent change to a protein's shape/function
  43. What are catalysts?
    Speed up the rate of reactions without being consumed (changed)
  44. What are enzymes?p
    Protein catalysts that permit low temperature reactions by reducing the activation energy (energy makes things happen).
  45. How are enzymes named after they bind with substrates?
    Most enzyme names end with "ase"
  46. Parts of an enzyme and their description.
    • 1) Active site: Site of reaction
    • 2) Substrate: Substance changed by enzyme, can be split or built (cata/anabolic)
  47. Induced fit model
    Enzyme active site squeezes down onto a specific substrate (1 enzyme for 1 substrate)
  48. Cofactors
    • Inorganic molecules
    •     - Bind to an enzyme to "activate" it
  49. Coenzyme
    • Organic molecules (from vitamins)
    •     - Bind to adjust the active site to receive the substrate
  50. What 4 things affect an enzyme's activity?
    • - pH level
    • - Substrate concentration
    •     - Enzyme concentration
    • - Temperature change
    • - Competitive inhibitors
  51. What happens to an enzyme when the pH level changes?
    Denatured or becomes not as efficient
  52. What is the effect of substrate concentration on enzyme activity?
    The increased number of substrates increases collisions, and therefore reactions, until no more enzymes are available.
  53. What is the optimum temperature for human enzymes?
    35° - 40°C (95° - 104°F)
  54. What happens to an enzyme at:
    1) Low temperatures
    2) As the temperature increases?
    3) At very high temperatures?
    • 1) Molecules move slowly
    • 2) Molecules move faster and reaction rates increases
    • 3) Enzyme structure is denatured
  55. Competitive inhibitors
    Competes for active site and mimics the substrate (renders enzyme useless)
  56. Allosteric activity
    Enzyme activity (its doing something)
  57. Feedback inhibition
    • Final product of a metabolic pathway, inhibits future production.
    • "Off switch"
  58. Precursor activity
    • Activating of the last enzyme by the initial reaction in the metabolic pathway, speeds up reactions.
    • "On Switch"
Author
Sehaj
ID
357670
Card Set
Unit 1(8): Digestion
Description
Biochemistry, Enzymes, Ingestion, Digestion
Updated