Biochem

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marshenski
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207305
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Biochem
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2013-03-16 12:45:28
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Boston College CRNA Biochem
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Boston College CRNA Biochem
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  1. What are the four categories of Biomolecules?
    • Proteins
    • carbohydrates
    • lipids
    • nucleic acids
  2. What are some processes that biomolecules are necessary for?
    • Breaking down food molecules
    • generating energy
    • storing energy (lipids)
  3. What are proteins?
    A series of amino acids, or polymers
  4. What are components make up an amino acid?
    Amine group and carboxylic acid group.
  5. What is the composition of a carbohydrate?
    either ketones or aldehyde with a hydroxide.
  6. What type of substances are lipids soluble?
    Non polar organic substances
  7. Classify the functional groups that would commonly be seen with a lipid.
    Non-polar
  8. What is the general structural "backbone" of nucleic acids made up of?
    Sugars
  9. What is the backbone of DNA?
    Deoxyribose
  10. What is the backbone of RNA?
    Ribose
  11. Define proteins
    large biological molecules of multiple amino acids linked via amide (peptide) bonds
  12. What type of proteins speed up reactions?
    Enzymes
  13. What is the function of urease? two enzymes were mentioned during the lecture and what are their functions?
    Urease: Catalyzes the hydrolysis of urea into Co2 and ammonia

    Acetylcolinesterase:breaks down acetylcholine
  14. What is an example of a storage protein?
    Myoglobin
  15. Give an example of a transport protein.
    hemoglobin
  16. What is an example of a structural protein?
    Collagen
  17. Name a type of protein that confers protection to our bodies?
    Immunoglobulin
  18. What are some examples of motion proteins?
    actin and myosin
  19. What allows proteins to have such a variety of functions?
    • They are linier polymers linked together
    • they have 3d strucures
    • they contain a variety functional groups
    • can also connect with other biochemical molecules
  20. What determines the function of proteins?
    3d structure
  21. What are the four parts of an amino acid?
    • central carbon
    • basic amino group
    • acidic carboxyl group
    • side chain
  22. In an amino acid, where is the alpha carbon?
    Adjacent to the carboxyl group.
  23. What determines the difference in amino acids?
    Various side chains
  24. How many total amino acids are there? How many are used to build proteins?
    300 and 20 respectively
  25. What determines 3d structure and charge on a protein?
    Various R groups
  26. True or false: A proteins often carry a charge.
    True
  27. What are two reasons proteins may not be able to cross the lipid bilayer?
    they are charged particles and they are quite large.
  28. All amino acids contain at least one asymmetrical carbon with the exception of what?
    glycine
  29. Jeopardy:
    The L- configuration
    What configuration do all naturally occurring proteins take?
  30. Why are amino acids naturally occurring in proteins only of the L-configuration?
    The enzymes that synthesize the proteins only insert the L amino acids in the chain.
  31. What is the primary structure of a protein?
    The specific amino acid sequence of the protein.
  32. By what process are proteins synthesized?
    Polymerization
  33. What is another name for a peptide bond?
    amide
  34. If polymer means plural then _______ means  singular.
    Monomer
  35. What molecule is liberated during the formation of a peptide bond?
    H2O
  36. Individual amino acids can be called what other name?
    amino acid residues
  37. When was the amino acid sequence of insulin discovered?
    1950
  38. Why was the sequencing of insulin an important discovery in biochemistry.
    It showed that a protein has a unique sequence of amino acids and they also discovered that the sequence of amino acids has a genetic basis.
  39. What makes up the regular and repeating patterns associated with secondary structure?
    hydrogen bonds that occur between backbone atoms of hydrogen and oxygen in neighboring segments of the chain.
  40. Bonds that create the secondary structure in a protein occur between what atoms?
    oxygen and hydrogen
  41. Which structure gives a protein its overall 3d shape?
    The tertiary structure.
  42. Folding of the polypeptide chain by tertiary structure occurs by what mechanism?
    bonding between R to R
  43. What does quaternary structure refer to?
    The way in which larger proteins come together to form larger aggregates.
  44. what is an important example of quaternary structure?
    hemoglobin.
  45. What reactions are associated with proteins?
    • Hydrolysis
    • denaturation
  46. What is hydrolysis?
    The breaking of peptide bonds via the introduction of water.
  47. What is the reverse of polymerization?
    Hydrolysis
  48. How are proteins digested?
    Hydrolysis
  49. When the primary structure of protein is not changed but any of the other secondary, tertiary or quaternary structures is changed, this is termed?
    denatured
  50. Can denatured proteins re-nature? he he
    The process is usually not reversible.
  51. What causes denaturing to occur?
    • Heat
    • Mechanical aggitation
    • Extremes of pH
  52. How many polypeptide chains are in hemoglobin, and what are their designations?
    4 total, 2 alpha-er and 2 beta-er (he he)
  53. What holds together the polypeptide chains of hemoglobin?
    various groups, specifically 4 heme units
  54. What does a heme unit consist of?
    Organic component containing a central iron atom
  55. How many units of O2 can a hemoglobin protein carry?
    4 (molecules/atoms)
  56. What substances causes blood to have its red color?
    Heme units
  57. What occurs to give sickle cells their distinct shape?
    Substitution of an amino acid.
  58. In hemoglobin A, what amino acid substitution will mutate it into hemoglobin S?
    valine is substituted for Glutamine to form the S variant.
  59. Is it the alpha or beta chains that is effected in sickle cell anemia?
    the beta chains
  60. How is can we determine the type of hemoglobin that a patient carry's?
    Electrophoresis
  61. Under what conditions is sickle cell trait inherited?
    Receiving hemoglobin A from one parent and hemoglobin S from the other.
  62. What is phenlkenonturia?
    Absence or deficiency of phenylalanine hydroxylase thereby leading to an accumulation of phenylalanine.
  63. What is phenylalanine normally converted to?
    Tyrosine
  64. How is phenylketonuria passed on?
    autosomal recessive transmission
  65. What is the treatment for phenylalanine?
    Low phenylalanine diet soon after birth
  66. What causes albinism?
    • Lack of enzyme tyrosinase
    • Lack of melanocytes and melanin
  67. In what fashion is albinism passed down?
    autosomal recessive
  68. What is a prion?
    A brain protein that converted to a proteinaceaous infectious particle.
  69. What specific change in protein structure makes prions infective?
    Changed in the secondary structure.
  70. How many of the "basic set of amino acids" can humans produce?
    11
  71. What do we call the 9 amino acids that humans can't produce and where do we get them?
    essential amino acids and we have to get them through our diet.
  72. From what amino acid precursor does histamine come?
    histidine
  73. From what amino acid precursor do thyroxine epinephrine, and melanin come from?
    tyrosine
  74. Why do epinephrine and thyroxine have similar side effects?
    because they both originate from tyrosine
  75. What is the problem with porphyria?
    there is a disruption in the pathway of heme sythesis
  76. What causes an accumulation of intermediates in the porphyrin pathway?
    Anything that induces an increase in heme requirements.
  77. What is the precursor to porphyrins?
    Glycine and succinly CoA (acetic acid/acetate)
  78. What determines the type of porohyria that is manifested?
    The specific enzyme deficiency in the chain
  79. What is the most serious form of porphyria?
    Acute intermittent porphyria
  80. How is acute intermittent porpyria passed on?
    autosomal dominant
  81. What is the goal of anesthesia when treating a pt with porphyria?
    Not provoke an attack
  82. When an attack of porphyria occurs how is it manifested and what is the pain often confused with?
    Sever abd pain and deficiencies in the CNS and PNS. Often mistaken as cholecystitis, pancreatitis, appendicitis, renal cholic.
  83. What happens to the nerves when a porphyria attack occurs?
    • Demyelination that results in:
    • -motor weakness
    • -diminished reflexes
    • -autonomic nervous dysfunction
    • -neuropathy
    • -impaired function of the cranial nerves
  84. What can occur intraoperatively with a porphyria pt?
    • labile hemodynamics
    • diaphoresis
    • arterial vasospasm
    • respiratory muscle paralysis
  85. What medications would we avoid with a pt who has porophyria?
    • barbituates
    • benzodiazepines
    • ketamine
    • etomidate
  86. What medications are "safe" with a porphyria pt?
    • narcotics
    • volitiles
    • muscle relaxants
  87. How does induction of the CYP450 enzyme precipitate in an attack of a porphyrin?
    Enzyme induction to CYP450 causes an increase in the requirements of the porphyirin pathway.
  88. T or F: Enzymes are mostly lipid soluble proteins.
    false
  89. How does an enzyme make a process more efficient?
    Decreases the energy of activation
  90. What is an enzymes function?
    to catalyze a reaction
  91. Fill in the blank. Enzymes are usually _____ and more _______ than inorganic catalysts.
    Bigger, complex
  92. In the absense of an enzyme are biological reactions fast or slow in general?
    Most biological reactions aren't perceptible without an enzyme to speed things up
  93. Do enzymes effect a wide variety of tissues?
    No, they are highly specific.
  94. What are three examples of enzymes brought up in class?
    • carbonic anhydrase
    • acetylcholinesterase or true cholinesterase
    • plasma cholinesterase or pseudocholinesterase
  95. What reaction does carbonic anhydrase catalyze?
    the hydration of CO2 and H2O into H2CO3 and the reverse reaction
  96. Carbonic anhydrase is the fastest known enzyme, How fast is it?
    It hydrates 1 million molecules a second and speeds up the reaction by 10 million times.
  97. What is the role of Acetocholinesterase?
    Splits acetylcholine into choline and an acetate ion
  98. Where is the site of acetylcholine release?
    • cholinergic neurons
    • neuromuscular junction
  99. What happens to the choline that has been split from acetylcholine?
    It is transported back into the cell for recycling.
  100. What substance does pseudocholinesterase break down?
    succinylcholine
  101. Where is pseudocholinesterase produced and where is it present?
    in the liver, in the blood plasma
  102. What happens to most of the dose of succ we give before it reaches the neuromuscular junction?
    It is broken down in the plasma by pseudocholinesterase
  103. How does Pseudocholinesterase breakdown the succ that reaches the neuromuscular junction?
    the succ will need diffuse back out of the junction to be broken down
  104. Which has a longer mechanism of action succinylcholine or acetylcholine and why?
    succ, because succ has to diffuse back out of the nm-junction prior to being broken down, and is essentially di-acetylcholine.
  105. What is the structure of succinylcholine?
    two acetylcholine molecules bound together. This binding makes the duration of action last longer.
  106. How is pseudocholinesterase deficiency passed down?
    "It's an inherited disorder."
  107. What does pseudocholinesterase deficiency or absence effect?
    Prolongs the response to succ
  108. Aside from the inherited form of pseudocholinesterase deficiency, who else has a decrease of this enzyme?
    • pt's with liver disease
    • pregnant pt's
  109. What is the relationship between substrate and enzyme concentrations?
    If there is a smaller number of substrate to enzyme then only some of the enzymes will be working. We can add additional substrate and increase the amount of reaction occurring until the numbers of substrate exceed that of the enzyme and then the reaction rate will reach a point where adding more substrate will not speed up the reaction.
  110. Is the reaction rate proportional or inverse to the number of enzymes available to react with substrate?
    Proportional
  111. Aside from concentration of substrate and enzyme, what other factors can effect the reaction rates?
    temperature and pH
  112. What is the ideal pH range in which enzymes work?
    5 - 9
  113. What two systems are responsible for regulating the chemistry of our bodies?
    the autonomic nervous system and the endocrine system, Neuro-endocrine control
  114. What are the chemical messengers of the endocrine system?
    Hormones
  115. What is the pathway of a hormone?
    secreting organ→blood→interstitial fluid surrounding organ→target organ
  116. Which of the nervous or endocrine system is faster?
    nervous
  117. How does the nervous system send its signals?
    mainly electrical signals but also neurotransmitters
  118. What are the two classifications of hormones?
    Protein derivatives or lipid derivatives
  119. What are the sub classes of protein derivatives?
    • amino acid derivatives
    • polypeptides
  120. What two general roles does epinephrine play in the body?
    hormone and neurotransmitter
  121. What are the largest class of hormones?
    polypeptides
  122. How many amino acids is TSH?
    108
  123. How many amino acids is insulin?
    51
  124. The lipid derivative hormones belong to which subclass?
    steroids
  125. Where are the control centers of the autonomic nervous system?
    • hypothalmus
    • the brainstem
    • spinal chord
  126. Why is it important to understand the autonomic NS?
    because many of the drugs that we use are stimulating or blocking portions of the ANS.
  127. What are the two divisions of the ANS neurons?
    presynaptic (preganglionic) and postsynaptic (postganglionic)
  128. How do the pre and post synaptic neurons communicate?
    the release and binding of neurotransmitters in the synaptic cleft
  129. How do the postsynaptic neuron a target tissues communicate?
    the release and binding of neurotransmitters in the neuromuscular junction
  130. To what what group do most of the neurotransmitters belong?
    amines
  131. What is the neurotransmitter of the presynaptic neurons?
    acetylcholine
  132. If a receptor is acted on by acetylcholine it a(n) ________ receptor?
    cholinergic
  133. In the parasympathetic NS, what is the neurotransmitter of the post synaptic neuron?
    acetylcholine
  134. In the sympathetic NS, what is the neurotransmitter of the post synaptic neuron?
    Norepinephrine
  135. If norepinephrine acts on a receptor it is a(n) __________ receptor?
    adrenergic
  136. What type of receptors do the β blockers and β agonist's bind to?
    Adrenergic
  137. What are the two types of cholinergic receptors?
    • Nicotinic
    • muscarinic
  138. Do the nicotinic and muscarinic receptors respond to the same neurotransmitter?
    Yes: acetylcholine but will act differently according to the receptor bound
  139. Where are the nicotinic receptors found?
    at the synapse between pre and post synaptic neurons in both the SNS and the PSNS; and at the neuromuscular junction of the SNS
  140. Where are the the muscarinic receptors found?
    in the end organs of the PSNS.
  141. In the ___ the preganglionic fiber is shorter than the postganglionic fiber.
    SNS it is the opposite in the PSNS
  142. What is the agonist to the muscarinic receptors?
    • acetylcholine
    • muscarine
  143. What are the antagonists of the muscarinic receptors?
    • Antimuscarinics:
    • -Atropine
    • -scopolomine
    • -glycopyrolate
  144. What are the agonists of the nicotinic receptors?
    • acetylcholine
    • Nicotine
  145. What are the antagonists of nicotinic receptors?
    • nondepolarizing muscle relaxants
    • ganglionic blockers:
    • -⇂bp
  146. Where do the ganglionic blockers block the action of acetylcholine?
    at the ganglia or neural synapse
  147. What is the goal of anesthesia in muscle relaxant reversal?
    maximize nicotinic transmission in the neuromuscular junction but to also give an antimuscarinic to block the effects of acetylcholine at the end organ.
  148. Acetylcholine binding to the muscarinic receptors in the heart would have what effect on the heart rate?
    decrease
  149. How does the drug Aricept work?
    it increases acetylcholine in the the brain
  150. What is the role of acetyl-SCoA in the the formation of acetylcholine?
    Acetyl-SCoA binds its Acetyl to choline to form acetylcholine
  151. What end organs have muscarinic receptors? (according to the slide 31)
    • glands: lacrimal, salivary, gastric
    • smooth muscle: bronchial, gastrointestinal, bladder
    • heart: SA node, AV node
  152. What is the only depolarizing muscle relaxer used in the US?
    Succinylcholine
  153. Are the nondepolarizing muscle relaxants agonists or antagonosts of acetylcholine?
    antagonists
  154. What is the onset of action of succinylcholine?
    30-60 seconds
  155. What is the duration of succinylcholine?
    normally less than 10 minutes
  156. What is the neurotransmitter for adrenergic receptors?
    mostly norepinephrine, but some do respond to epinephrine
  157. Where is norepinephrine synthesized?
    in the cytoplasm
  158. Where is norepinephrine released?
    by exocytosis from the postganglionic fibers
  159. How is the action of norepi terminated?
    • taken back into the postganlionic nerve endings
    • diffusion away from the receptor
    • metabolism by monoamineoidxidase
    • metabolism by (COMT) catechol-o-methyltransferase
  160. How do tricyclic antidepressants effect norepi?
    inhibit reuptake into the postganglionic nerve fiber
  161. How does an MAOI work?
    inhibition of the metabolism of norepi by monoamineoxidase
  162. What are the two divisions of the adrenergic receptors?
    Alpha and Beta
  163. What are two drugs that we use for intraop control of bp?
    • Ephedrine
    • Phenylephrine
  164. What receptor does phenylephrine act on mainly?
    α1
  165. Phenylephrine is an _____ agonist.
    alpha
  166. What receptors does ephedrine work on?
    both alpha and beta
  167. Giving a pure alpha agonist will result in what? (in regards to anesthesia)
    increasing blood pressure and a decrease in heart rate.
  168. What type of pt would we give ephedrine to?
    a patient with an elevated hr and low bp
  169. When would we give phenylephrine to a pt?
    hypotension with bradycardia
  170. What are three susbstances that directly activate the adrenergic receptors?
    • epinephrine
    • norepinephrine
    • phenylephrine
  171. What is a direct acting agent?
    one that binds directly to a receptor
  172. What is an indirect acting agent?
    one that depends on release of endogenous catecholamines and the catecholamines activate the receptor
  173. What is a mixed acting Drug and give an example?
    one that both stimulates a receptor directly but also will cause a release of catecholamines to activate the receptor. Ephedrine
  174. What prevents ephedrine from being a purely direct acting agent?
    it is missing the OH group on it benzene ring
  175. What prolongs the effect of ephedrine?
    the extra methyl group block the action of MAO
  176. What amino acid is histamine derived from?
    histadine
  177. What are some medications that will cause a release of histamine?
    • thiopental
    • succ
    • morphine
    • atracurium
  178. What drugs would we want to avoid if the pt is on an H2 blocker?
    • Thiopental
    • succ
    • morphine
    • atracuruim

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