Lecture 1

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Anonymous
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90096
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Lecture 1
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2011-06-10 17:57:26
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Molecular cellular respiration
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molecular and cellular respiration
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  1. _________ shape of both the enzyme and substrate are altered upon binding.
    induced fit
  2. quaternary structure
    When 2 or more polypeptide chains bind together. Same 5 forces in the tertiary structure can also act to form the quaternary structures
  3. Krebs cycle products
    1 glucose = 2 turns

    each turn = 1 ATP, 3 NADH, 1 FADH2
  4. _______ solvent in w/c the chemical rxns of living cells take paces. 70-80% of a cell's mass is due to this. Small polar molecult
    Water
  5. They are called ___ because the amine is attached to the carbon in the alpha position of the carbonyl approx______ of them
    alpha- AA

    20
  6. In typical DNA, two strands are joined by hydrogen bonds to make the structure called a _______
    double helix
  7. ______ any biological molecule that has low solubility in water and high solubiility in nonpolar organic solvents
    lipid
  8. The proton-motive force propels thru______ to manufacture ATP.
    ATp syntase
  9. ________ dissolved inorganic ions inside and outside the cell.
    -create electrochemical gradients.
    -Combine and solidify to give strength to a matrix such as hydroxyapatite in bone
    - cofactors, assisting enzyme or protein function
    Minerals
  10. _______-intermolecular bond allows water to be a liquid at typical cell temps strong cohesive forces between water molecules
    Hydrogen bond
  11. Denaturing agent and forces disrupted-
    • Urea- hydrogen bonds
    • salt or change in pH- electrostatic bonds
    • mercaptoethanol- disulfide bonds
    • Organic solvents- hydrophobic forces
    • heat- all forces
  12. ______ agents which bind covalently to enzymes and disrupt their function. (usually high toxic, penicillin in an example.
    irreversible inhibitors
  13. made from carbon and water, empirical formula C(H2O)
    Carbohydrates or sugars or saccharides
  14. _______ feedback inhibitors bind to the enzyme and cause a conformational change. both _______ inhibitor and ______ activator.
    Allosteric regulation.
  15. Combustion reaction
    • not balanced :
    • glucose + O2 ---> CO2 + H2O
  16. Plants form ____ from glucose
    Cellulose has ______ linkages.

    Cows and termites etc have bacteria in their digestive system that release an enzyme to digest the ____ linkages
    Starch

    Beta

    beta
  17. _____ a coenzyme which transfers 2 carbons (from pyruvate) to the 4- carbon oxaloacetic acid to begin the krebs cycle/also called the citric acid cycle.
    acetly-coa
  18. ____ increases the rate of diffusion for glucose and other monosaccharides
    insulin
  19. _______ fluid portion of living cells
    Cytosol
  20. nucleotides
    • composed of 3 components:
    • 1. a 5 carbon sugar
    • 2. a nitrogenous base
    • 3. a phosphate group
  21. _____ this chemical is an enzyme and therefore probably a protein and therefore contains nitrogen and is subject to denaturation
    -ase
  22. other important nucleotides
    ATP- source of readily available energy for the cell

    Cyclic amp- important component in many 2nd messenger systems

    NADH & FADH2- the coenzymes involved in kerbs cycle.
  23. _______ anaerobic respiration, includes the process of glycolysis the reduction of pyruvate to ethanol or lactic acid, the oxidation of the NADH back to the NAD+

    recycles NADH back to NAD+
    Fermentation
  24. ______if one of the products downstream in a reaction series comes back and inhibits the enzymatic activity in an earlier rxn.

    If it works it shuts off, like a thermostat
    negative feedback or feedback inhibition
  25. nucleic acids
    • DNA and RNA
    • formed from the nucleotides
  26. Hydrophobic
    water fearing nonpolar
  27. _____ non consumes or permanently altered by the reaction, only a small amount required. do not alter the _____ of a reaction.
    Catalyst (enzyme) equilibrium
  28. Hydrophilic
    water loving polar like dissolves like
  29. ______only 1 strand and no helix is formed and uracil replaced thymine
    RNA
  30. ______the position on the enzyme to where the substrate binds, usually with numerous non-covalent bonds.
    active site
  31. _____are built from a chain of amino acids linked together by peptide bonds.
    proteins (polypeptides)
  32. ________ a lipid. building blocks for most, but not all complex lipids. long chain of carbons truncated at one end by a carboxylic acid. Usually an even # of crbons with the max in humans being 24
    fatty acids
  33. glycerol
    3 carbon backbone
  34. _____ glycerol backbone, with 2 fatty acids and a polar phosphate group with lies on opposite end of the nonpolar fatty acids.
    phospholipid
  35. ______organic molecule many are vitamins or their derivatives.
    coenzymes
  36. krebs cycle or citric acid cycle
    • each turn of the krbs cycle produces: 1 ATP, 3 NADH, and 1 FADH2.
    • During the cycle 2 carbons are lost and CO2 and oxaloacetic acid is reproduced to begin the cycle over again.
  37. essential amino acids
    (10) amino acids that the body can't manufacture, must be ingested
  38. ______ production of ATP by the proton motive force thru ATP synthase
    Oxidative phosphorylation
  39. ______polysaccharide, branches glucose polymer with alpha linkages most is found in the liver and muscle cells
    glycogen
  40. VLDL-

    LDL-

    HDL-
    very low density lipoprotein

    low density lipoprotein

    high density lipoprotein
  41. Respiration-
    steps 2 and 3 of metabolism

    • W/ oxygen - aerobic
    • w/0 oxygen- anaerobic
  42. _____bind nonvovalently to an enzyme at a spot other than the active site and change the conformation (shape) of the enzyme. so the substrate does not even fit in the active site anymore
    non competitive inhibitors
  43. Unsaturated fatty acids
    contain one or more C=C.
  44. ____ typ a globular protein occasionally a nucleic acid, act as a catalyst by lowering the activation energy and increasing the reaction rate ( by magnitudes as much as thousands of trillions)
    enzymes
  45. _______example of enzyme specificity. Active site of the enzyme has a specific shape that only fits a specific substrate.
    lock and key theory

    enzyme= lock

    substrate= key
  46. The enzyme bound to the substrate is called _______
    enzyme- substrate complex
  47. _______each amino acid in a polypeptide chain
    residue
  48. Water molecules surround ______ a hyrophilic molecule and separate it form the group
    Solvate
  49. Lipid functions

    Phosopholipids-
    triacylglycerols-
    fatty acids (eicosanoids)-
    steroids-
    • structural component of membranes
    • store metabolic energy, provide thermal insulation & padding
    • serve as local hormones
    • regulate metabolic activities
  50. amphipathic
    • one end is polar
    • one end is nonpolar
    • eg. phospholipid
  51. 5 forces creating the tertiary sturcture
    • 1. covalent disulfide bonds b/n two cysteine AA on different parts of the chain.
    • 2. electrostatic (ioni) interactions mostly b/n acidic and basic side chains.
    • 3. hydrogen bonds
    • 4. van der waals forces
    • 5. hydrophobic side chains pushed away from water (toward center of protein)
  52. inactive form of an enzyme, depending, they can reversibly or irreversibly activated
    zymogen or proenzyme
  53. most macromolecules of living cells are broken apart via_________
    hydrolysis
  54. ________ how most macromolecules are formed
    dehyration synthesis
  55. _________ the reactant or reactions upon which the enzyme works. Generally _______ than the enzyme
    substrates

    smaller
  56. Aerobic respiration products
    approx 36 net ATP

    1 NADH bring back 2 to 3 ATP

    1 FADH2 bring back aprx 2 ATP
  57. denatured (proteins)
    lost most of its secondary, tertiary and quaternary structure

    often once the denaturing agent is removed the protein will spontaneously refold to its original conformation
  58. ________ a non-proetin component that many enzymes require. can be coenzymes or metal ions (mineral)
    Cofactor
  59. ______ normally, enzymes are designed to work only on a specific substrate or group of closely related substrates
    enzyme specificity
  60. __________ the first substrate changes the shape of the enzyme allowing other substrates to bind more easily.
    Positive cooperativity, negative cooperativity is the opposite.
  61. _____ four ringed structure, includes some hormones, vitamin D and cholesterol
    Steroids
  62. On MCAT when you see nitrogen
    think of protein
  63. ______ what the single chain can form
    _______ are secondary structure
    alpha-helix

    beta-plated sheet
  64. inner mitochondrial membrane
    less permeable than the outer.

    have to pass thru to get to the mitochondrial matrix
  65. ________ the process of ATP production in the krebs cycle.
    substrate level phosphorylation
  66. _______a 6th class of lipids which include vitamin A.
    Terpenes
  67. In nucleic acids, nucleotides are joined together by _____between the phosphate groups of 1 nucleotide and the 3rd carbon of the pentose of the other nucleotide forming long strands.
    phospodiester bonds
  68. _______ (substrate has to wait in line on enzymes) As the relative concn. of substrate increases the rate of the reaction also increases but less and less until a max rate (Vmax) is achieved.
    Saturation kinetics
  69. _____ 6 carbon carbohydrate C6H12O6, very common accounts for 80% of the carbohydrates absorbed by humans
    glucose
  70. ______ 3D shape formed when the peptide chain curls and folds
    tertiary structure
  71. _____ the products of glycolysis move here past both membranes
    matrix of mitochondrion
  72. metabolism-
    • all cellular chemical reactions.
    • consists of anabolism, molecular synthesis and catabolism
  73. intermembrane space has______
    lower pH than the matrix
  74. most common nitrogenous base
    thymine (uracil)

    • Adenine
    • guanine
    • cytosine
  75. Rxn rate______ with pH, temp and substrate concn.
    • moderates, bell curve shape.
    • moderates, bell curve shape but with a slight nudge towards higher temps.
    • logarithmic, point at which higher conc= no gains
  76. ______ the number and sequence of amino acids in a polypeptide
    primary structure
  77. Aerobic respiration___
    requires oxygen
  78. Glycolysis
    • 2 stages, 6 carbon and 3 carbon stage
    • 6 expends 2 ATPs to phosphorylate the molecule
    • 3 synthesizes 2 ATP with each 3 carbon molecule (2 net positive)
    • 2 pyruvate and 2 NADH molecules left and 2 Net ATP (4 actual)
  79. _______ (3 names)
    has a 3 carbon backbone called a glycerol, which is attached to 3 fatty acids function is to store energy and may provide thermal insulation and may provide padding
    • triglycerides
    • or fats and oils

    or triacyglycerols
  80. side chain (r group)
    • how AA typically differ from each other
    • this side chain is also attached to the alpha carbon
  81. ____ compete with the substrate by binding reversibly with noncovalent bonds to the active site. (usually only for a fraction of a second)
    competitive inhibitors
  82. In the matrix, pyruvate is converted to this _____ in a reaction that produces NADH and CO2
    Acetylcoa
  83. _______ a series of protein including cytochromes with heme in the inner membrane of the mitochondrion
    electron transport chain (ETC)
  84. _____ or _____
    specialized cells whose cytoplasm contains almost nothing but triglycerides
    • adipocytes
    • fat cells
  85. _______ contains a lipid core surrounded by phospholipids and apoproteins can dissolves lipids in its hydrophobic core and move freely in aqueous solution due to its hydrophilic shell
    lipoproteins
  86. _______ is the modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme
    allosteric interaction
  87. Glycolysis
    • 1st stage of anaerobic and aerobic respiration,
    • breaks down glucose into 2 3-carbon molecules of pyruvate (conj. base of pyruvic acid)

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