Anatomy Chapter 2 Review

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  1. 98.5% of body weight consists of
    C, O, H, N, Ca, P
  2. 96% of body weight consists of
    C, O, H, N
  3. Element
    pure substance
  4. Atom
    smallest unit in an element
  5. Compound
    two or more elements joined in definite porportions
  6. Molecule
    smallest unit of a compound
  7. What determines chemical behavior
    electrons
  8. Isotopes
    same chemical behavior, differ in physical behavior
  9. Radioisotopes
    unstable isotopes
  10. Radiation from radioisotopes cause
    damage to molecules and cause free radicals (cause aging)
  11. Free Particle
    A particle with an odd number of electrons
  12. Antioxidants and examples
    neutralize free radicals, examples vitamin E, Vitamin C,  carotenoids, SOD
  13. Ionic Bond
    transfer of electrons
  14. Covalent Bond
    Sharing of electrons
  15. Hydrogen Bond
    Weak electrostatic bonds
  16. Van der Waals forces
    same as hydrogen bonds
  17. Electrolytes
    salts that ionize water, conduct electricity
  18. Bodys most abundant electrolytes
    Na+, Ca2+. Mg2+, Cl-, PO4-3, and HCO3-
  19. Non-polar covalent bond
    share equally (strongest bond chemically)
  20. Polar covalent bond
    share unequally
  21. Properties of water and mixtures
    solvency, cohesion, adhesion, chemical reactivity, thermal stability, pH acid
  22. Solvency
    ability to dissolve matter
  23. Hydrophillic
    charged substances that easily dissolve in water
  24. Hydrophobic
    neutral substances that do not easily dissolve in water
  25. NaCl what keeps them from coming in contact after being exposed to water
    Hydration Spheres
  26. Heat Capacity
    amount of heat required to raise the temperature of 1g of a substance by 1 degree C
  27. Calorie
    amount of heat required to raise the temperature of 1g of water by 1 degree C
  28. Water effective as a coolant
    1ml of perspiration removes 500 calories from the body
  29. Types of Mixtures with Water
    Solutions, Colloids, and Suspensions
  30. Solutions
    less than 1nm, pass through membranes, transparent, e.g. copper sulfate solution, will not separate on standing
  31. Colloids
    between 1nm to 100nm, too large to pass through membranes, does not separate on standing, cloudy, e.g. milk, blood proteins, water
  32. Suspensions
    particles larger than 100nm, cloudy or opaque, separates on standing, e.g blood cells
  33. Mole or Avagadro Number
    6.02 x 1023 one mole
  34. Acid
    Acid is a proton donor
  35. Base
    base is a proton acceptor
  36. Buffers
    resist any change in pH helps keep blood in check
  37. Blood pH
    7.34-7.45
  38. Stomach, Acid or Base?
    acidic
  39. Pancreatic solutions, Acid or Base
    basic
  40. Energy
    the capacity to do work
  41. Classes of reactions
    Decomposition, Synthesis, Exchange
  42. What speeds up reaction rates
    Concentration, temperature, catalyist
  43. Metabolism
    is the sum of all chemical reactions in the body
  44. Catabolism
    energy releasing decomposition reactions
  45. Anabolism
    energy consuming synthesis reactions
  46. Four classes of organic molecules
    Carbohydrates, lipid, proteins, nucleotides, nucleic acids
  47. Functional groups
    Groups of atoms attached to carbon backbone, determine the properties of organic molecules, all are hydrophillic except methyl group
  48. Name all functional groups
    Hydroxl OH-sugars, alcohol, Methyl-CH3-amino acids, fats, oils, steroids, Carboxyl COOH-amino acids, sugars, proteins, Amino NH2-amino acids, proteins, Phosphate H2PO4-ATP, nucleic acids
  49. How many monomers does DNA have
    4 monomers (nucleotides)
  50. How many monomers do proteins have
    20 different monomers (amino acids)
  51. Dehydration Synthesis
    monomers bind together to form a polymer with the removal of a water molecule
  52. Hydrolysis
    splitting a polymer with the addition of a water molecule
  53. Three Dissaccharides
    Sucrose, Lactose, Maltose
  54. Sucrose combination
    glucose + fructose
  55. Lactose combination
    galactose + glucose
  56. Maltose combination
    glucose + glucose
  57. Polysaccharides
    starch, cellulose, glycogen
  58. What is produced by plants and how digested
    starch digested by amylase
  59. What is glycogen
    is an energy storage polysaccharide produced by animals, stored in liver
  60. Glycolipids
    external surface of cell membrane
  61. Glycoproteins
    external surface of cell membrane (mucous of respiratory tract and digestive tract)
  62. Proteoglycans
    carbohydrate component dominant in cell adhesion, gelationous filler of eye tissues
  63. Lipids
    hydrophobic organic molecule
  64. All five primary types of lipids
    fatty acid, triglyceride, phospholipids, eicosanoids, steroids
  65. Fatty Acids
    chain of usually 4 to 24 carbon atoms
  66. Triglycerides (are called neutral fats)
    three fatty acids bonded to glycerol by dehydration synthesis
  67. Phospholipids (both hydrophillic and hydrophobic)
    similar to triglycerides but one fatty acid is replaced by a phosphate group
  68. Eicosanoids
    derived from arachidonic acid (20 carbon chain) hormone like chemical signals locally between cells includes prostaglandins
  69. Steroids
    cholesterol, parent steroid fro which other steroids are synthesized. Synthesized only by animals, 85% produced naturally in our liver and 15% from diet
  70. Cholesterol
    4 ringed structure all steroids have
  71. Amino acids
    proteins contain many amino acids, non-polar r groups are hydrophobic, polar r groups are hydrophillic
  72. Peptides
    a polymer of 2 or more amino acids
  73. Oligopeptides
    have fewer than 10 to 15 amino acids
  74. Polypeptides
    have more than 15 amino acids
  75. Proteins
    have more than 50 amino acids
  76. Primary Structure of Protein
    determined by amino acid sequence
  77. Secondary Structure of Protein
    coiled or folded shape held together by hydrogen bonds, alpha helix coiled, beta pleated folded
  78. Tertiary Structure of Protein
    interaction of large segments to each other and surrounding water, provides 3d structure to the protein. (globular proteins soluble, fibrous proteins insoluble)
  79. Quaternary Structure of Proteins
    two or more polypeptide chains interacting
  80. Hemoglobin
    made up of four separate chains with a heme group on each chain
  81. Protein Conformation
    overall 3-d shape is crucial to function
  82. Protein Functions
    Structure, Communication, Membrane Transport, Catalysis, Recognition and protection, Movement, Cell Adhesion
  83. Substrate
    the substance an enzyme acts upon
  84. Products
    are formed from the reaction
  85. Cofactors
    minerals in diet e.g iron, zinc, copper, magnesium
  86. What are the monomers of Nucleic Acids
    nucleotides
  87. Nucleic Acids
    polymers of nucleotides
  88. DNA
    100 million to 1 billion nucleotides long, responsible for cell division, sexual reproduction, protein synthesis
  89. RNA
    3 forms of RNA range from 70 to 10000 nucleotides long, carries out instructions given by DNA
  90. Nucleotides Monomers
    Nitrogenous base, sugar, phosphate
  91. ATP Glucose
    produce 38 ATP per glucose molecule
  92. GTP
    Guanosine triphosphate, may donate a phosphate group to ADP
  93. cAMP
    Cyclic Adenosine Monophosphate, after chemical signal binds to cell surface, triggers conversion of ATP to cAMP, cAMP turns on/off effects inside cell
  94. What type of bond is a weak electrostatic attraction between molecules?
    Ionic bond
  95. What type of bond involves unequal sharing?
    Polar bond
  96. What type of bonding gives water its many unique properties?
    Hydrogen bonding
  97. A positive ion is called a?
    Cation
  98. A negative ion is a?
    Anion

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TopShot102
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Filename:
Anatomy Chapter 2 Review
Updated:
2017-02-14 04:34:17
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Test 2
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