Eng Bio Macromolecules of Life Notes

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  1. Name 3 reasons carbohydrates (sugars) are important.
    • 1) Source of energy for driving cellular metabolism
    • 2) Chemical Signaling
    • 3) Structure – insect exoskeleton, cellulose
  2. Name 2 reasons lipids are important.
    1) Lipids or long chain hydrocarbons are used for structure (relatively small)

    2) Collections of lipids form membranes in an aqueous environment (van der Waals, hydrophylic/hydrophobic interactions)
  3. True or False: Macromolecules as covalent bonds do not hold adjacent lipids together.
  4. What do membranes do in cells?
    Membranes separate cells and make compartments within cells.
  5. Why are proteins important?
    Proteins make up the molecular machinery of cells and they are polymers of 21 different amino acids.
  6. Proteins make up the molecular machinery of what kinds of cells?

    A) None of these
    B) Structure cells
    C) Antibodies
    D) Transport proteins
    E) Enzymes
    F) All of these
    F) All of these
    (this multiple choice question has been scrambled)
  7. Why are nucleic acids important?
    They carry information.
  8. What are nucleic acids made of?
  9. How many different nucleic acids are used in the coding of DNA and RNA?
  10. What are two types of codes formed from different nucleic acids?
    DNA and RNA
  11. Define Stereoisomers
    • Molecules with the same chemical composition but different arrangement of atoms about an
    • asymmetric, or chiral, carbon
  12. In a biological system with two stereoisomers, what is the status of these stereoisomers?
    Most commonly one stereoisomer is active within a system and the other is not.
  13. Dextro (D) represents what kind of stereoisomer?
    One that is active in a biological system.
  14. Levo (L) represents what kind of stereoisomer?
    One that is inactive in a biological system.
  15. What are the roles of sugar?
    1) Structure (cellulose)

    2) Storage/energy

    3) Signaling
  16. What is the basic unit of a sugar?
  17. What is the name of a monosaccharide with 6 carbons?
  18. What is the name of a monosaccharide with 5 carbons?
  19. What is the name of a monosaccharide with 4 carbons?
  20. What is the name of a monosaccharide with 3 carbons?
  21. What are the two chemical categorizations of monosaccharides?
    Aldose and Ketose
  22. Give an example of an Aldose.
  23. Give an example of a Ketose.
  24. How many carbons does Glucose have?
  25. What is the structure of ribose?
    Furan ring structure
  26. How many carbons does Ribose have?
  27. What are the 2 forms of ribose?
    Ribose and Deoxyribose
  28. Glucose + Glucose = ?
  29. What kind of linkage between glucose molecules forms Maltose?
    Image Upload –1,4 glycosidic linkage
  30. The formation of Maltose from 2 Glucose molecules is what type of reaction?
    Condensation Reaction
  31. What is sucrose?
    Table Sugar
  32. What is Lactose?
    Milk Sugar
  33. How is lactose formed?
    Image Upload–1,4 glycosidic linkage
  34. What are polysaccharides?
    Very large, complex molecules made up of sugars.
  35. What causes the complexity of polysaccharides?
    The ability of monosaccharides to bind in many ways
  36. What is amylose?
    Part of starch
  37. How is amylose formed?
    Multiple Image Upload–1,4 glycosidic linkages
  38. What is Chitin?
    Insect Exoskeleton
  39. How is chitin formed?
    Multiple Image Upload–1,4 glycosidic linkages
  40. How is cellulose formed?
    Multiple Image Upload–1,4 glycosidic linkages
  41. True or False: Cellulose is digestible by humans.
  42. How is glycogen formed?
    Multiple Image Upload–1,4 glycosidic linkages
  43. True or False: Glycogen is digestible by humans.
  44. How are polysaccharides stored?
    They are stored in muscles and liver as secondary Energy storage.
  45. Why are polysaccharides stored in muscles?
    For immediate use in muscles
  46. Why are polysaccharides stored in the liver?
    For distribution systemically
  47. Name the sources of starch.
    Potatoes and Corn
  48. Name the uses of starch.
    Food and Clothing
  49. Name the sources of cellulose.
    Wood and Cotton
  50. Name the uses of cellulose.
    Paper and Clothing
  51. Name the source of carrageenan.
    mycophyta (algae)Name the sources of starch.
  52. Name the use of carrageenan.
  53. Name the source of agar.
    mycophyta (algae)
  54. Name the uses of agar.
    Microbiology and Food
  55. Name the source of dextran.
  56. Name the uses of dextran.
    Food and Medicine
  57. Name the source of agarose.
    mycophyta (algae)
  58. Name the use of agarose.
  59. Name the source of xanthan gum.
    X. campestris
  60. Name the uses of xanthan gum.
    Food, industrial chemical, and oil field drilling
  61. Define Lipids
    Category of hydrophobic compounds that are insoluble in water but soluble in nonpolar solvents.  Present in nonaqueous phases of cells
  62. Define Fats
    Combined lipids that serve as biological energy storage molecules.
  63. Define Steriods
    Hormones that are regulators/stimulators of many cellular functions at low concentrations. Complex in structure.
  64. What is the main component of lipids?
    Fatty Acids
  65. A lipid typically consists of how many carbons?
    12-20 Carbons
  66. What are the 2 components of a fatty acids?
    A strongly nonpolar hydrocarbon chain and a polar terminal group.
  67. What does it mean if a lipid/fatty acid is saturated?
    It means it has the max number of H atoms and is linear.
  68. What does it mean if a lipid/fatty acid is unsaturated?
    It means there are some C=C bonds present. The chain is kinked and has a cis/trans configuration.
  69. Which is more saturated? Lard or Olive Oil?
    Lard is more saturated. Lard is 37.7 % saturated while olive oil is only 2.9 % saturated. However, olive oil is considered very saturated so Lard is even more saturated than that.
  70. What is the hydrogenation of oils?
    Add H2 to liquid oil under pressure.
  71. Why do we hydrogenate vegetable oils?

    a) So it does not turn rancid as fast (improve shelf life)
    b) To make them solid/semisolid at room temperature
    c) To increase the temperature at which they
    d) All of these
    e) None of these
    d) All of these
  72. Fatty acids naturally occur in which form primarily?

    a) cis
    b) trans
    a) cis
  73. Which orientation of the H atoms occurs as a result of the hydrogenation process?

    a) cis
    b) trans
    b) trans
  74. What is a phospholipid?
    Its an important component of cell membranes.
  75. What are phospholipids composed of?
    2 Fatty Acids, glycerol, 1 Phosphate, and 1 Choline or Other Group

    Image Upload
  76. What is this structure?

    Image Upload
    Phosphatidic Acid
  77. What is this structure?

    Image Upload
  78. What are the two types of structures commonly formed by phospholipids?
    phospholipid double Layers and single layer micelles
  79. What are triglycerides?
  80. What is the equation for fats/triglycerides?
    Fats = 1 Glycerol + 3 Fatty Acids

    (The fatty acids can be different.)
  81. What is the precursor to steriods?
  82. What are naturally occuring steroids?

    A) none of these
    B) hormones
    C) fats
    D) lipids
    B) hormones
    (this multiple choice question has been scrambled)
  83. Where does cholesterol occur?
    In membranes.
  84. What is the purpose of the steroid Cortisone?
  85. What is this structure?

    Image Upload

    (precursor for many steroids including testosterone and cortisone)
  86. What is this structure?

    Image Upload

    (an adrenocortical hormone)
  87. What is this structure?

    Image Upload

    (a female sex hormone)
  88. What is this structure?

    Image Upload

    (a male sex hormone)
  89. What is this structure?

    Image Upload
  90. What are the building blocks of polypeptides and protein?
    Amino Acids
  91. Which amino acid isomer is found in proteins and is most common.
    L isomer
  92. Which group varies to form different amino acids?
    The R Group
  93. Which form of amino acids are found primarily in bacterial cell walls?
    D form
  94. Ionization states of an amino acid depend on

    A) the R group
    B) pH
    C) size
    D) temperature
    B) pH
    (this multiple choice question has been scrambled)
  95. How many amino acids are found in proteins?
    21 amino acids
  96. How many amino acids are encoded in the human genome?
    All 21 of the amino acids which are found in proteins
  97. How many amino acids are essential to humans?
    9 amino acids
  98. Name the amino acids essential to humans.
    Histidine, Isoleucine, Leucine, Lysing, Methionine, Phenylalanine, Threonine, Tryptophan, and Valine
  99. What are polymers formed of amino acids?
  100. If a polypeptide chain ends with a Nitrogen, it is said to be

    a) amino terminus
    b) carboxy terminus
    a) amino terminus
  101. If a polypeptide chain ends with a Carbon, it is said to be

    a) amino terminus
    b) carboxy terminus
    b) carboxy terminus
  102. Polypeptides/proteins are formed via what reaction?
    A condensation reaction
  103. What kind of bond forms between amino acids?
    A peptide bond
  104. How many levels of protein structure are there? What are they?
    4 levels

    Primary, Secondary, Tertiary, and Quaternary
  105. What is primary protein structure?
    Sequence of amino acids (ie Leu, Val, Cys, Met)

    Held together by covalent bonds between amino acids (peptide bond, amide linkage)

    Proteins synthesized by cells only have peptide bonds and nothing synthesized onto R groups.  Protein production only makes the covalent bonds between amino acids.
  106. What is secondary protein structure?
    Results from H bonding between amino acid residues on the same peptide backbone.

    Bonding is between N and O.

    Common examples of secondary structure are α-helix, β-pleated sheet, triple α-helix (collagen)
  107. What is tertiary protein structure?
    Results from interactions between R (and other) groups widely separated on the polypeptide chain.

    Disulfide bonds S-S (Cys-Cys)

    Covalent bonds

    Hydrophobic-hydrophylic interactions

    Also results from interactions between α-helix and β-pleated sheet
  108. Which factors are included in tertiary structure?
    Surface Properties, Catalytic Activity, Chemical Stability, Shape, and Mechanical Strength
  109. Which protein structure level is dependent on how the protein is synthesized?
  110. How are procaryotes synthesized?
    This type of protein is synthesized in the cytoplasm and tertiary structure develops as it is made.  No ER for posttranslational modification.
  111. How are eucaryotes synthesized?
    Rough ER may tether protein end while it is being made.  Modifications can happen while the protein is held by the ER; these can effect structure.
  112. What is quaternary protein structure?
    Results from interactions between more than one polypeptide chain

    2 or more chains

    Many proteins have multiple subunits
  113. True or False: The majority of proteins are pure.
    False. The majority of Proteins are not “pure” but are conjugated to some other molecule
  114. What is the name of the cellular process used to modify proteins into conjugates after they have been made?
    posttranslational modification
  115. What is is the moiety conjugated to the protein?
    The Prosthetic Group
  116. What are the classes of modified proteins?
    Lipoproteins, Glycoproteins, Phosphoprotein, Hemoproteins, Flavoproteins, and Metalloproteins
  117. What is the prosthetic group for lipoproteins?
  118. What is the prosthetic group for glycoproteins?
  119. What is the prosthetic group for phosphoproteins?
  120. What is the prosthetic group for hemoproteins?
    Iron Porphyrin
  121. What is the prosthetic group for flavoproteins?
    Falvin Nucleotides
  122. What is the prosthetic group for metalloproteins?
    Iron and Zinc
  123. Give an example of lipoproteins.
    B-lipoprotein of blood
  124. Give an example of glycoproteins.
    Gamma Globulin
  125. Give an example of phosphoproteins.
    Protein Kinase C
  126. Give an example of hemoproteins.
  127. Give an example of flavoproteins.
    Sucinate dyhydrogenase
  128. Give an example of metalloproteins.
    Alcohol dehydrogenase
  129. What are antibodies?
    A specific class of proteins produced by B cells of the blood.
  130. There are many types of antibodies but what is most common example in protein chemistry?
  131. Antibodies are made of how many chains?
    4 chains (2 heavy chains and 2 light chains)
  132. There are variable regions on the ends of antibodies made for what purpose?
    To specifically bind foreign objects
  133. Proteins in which categories are commercially produced?
    Structural, Enzymes, Transport, Nutrient, Contractile, Defense, Regulatory, and Inhibitors
  134. Name some structural proteins.
    Keratin (skin)

    Fibroin (silk)

    Collagen (tendons & ligaments)

    Elastin (joints)

    Proteoglycans (cell walls)
  135. Name some enzymatic proteins.
    Trypsin (cleaves proteins)

    DNA polymerase (makes DNA)

    Cellulase (breaks down cellulose)

    peroxidase (reagent)
  136. Name some transport proteins.
    Hemoglobin (transfers oxygen)

    Na/K ATPase (moves K and Na)
  137. Name some nutrient storage proteins.
    Ovalbumin (egg)

    Casein (milk)
  138. Name some contractile or motile proteins.
    Actin (muscle)

    Myosin (muscle)

    Tubulin (cytoplasm)
  139. Name some defense proteins.
    Venom proteins (for producing antivenom)

    Ricin and others (biodefense)
  140. Name some regulatory proteins.
    Human Growth Hormone


    Cytokines (cancer treatment)

    Protein Kinases (signal transduction)

    Insulin like growth factor

    Other hormones (testosterone, estrogen…)
  141. Name some inhibitor proteins.
    Trypsin inhibitor (reagent)

    HIV protease inhibitor
  142. Name some therapeutic agent proteins.
    Antibiotics (many types)

  143. What does it mean for a protein to denature?
    It means that one of the levels of structure has been altered relative to the normal functional state
  144. Protein function is most dependent on what?
    Function is most dependent on quaternary and tertiary structure which both depend on secondary and primary structure
  145. Why is it important to preserve the integrity of the protein through processing and separation?
    Because a denatured protein generally loses function
  146. What force can denature a protein?

    A) None of these
    B) pH
    C) All of these
    D) Shear
    E) Temperature
    C) All of these
    (this multiple choice question has been scrambled)
  147. What are the monomers of DNA?
  148. What is the general formula for DNA?
    DNA = sugar + base + phosphate

    (Sugars include ribose and deoxyribose)
  149. What are the two types of bases in DNA?
    Purine (double ring) and Pyrimidine (single ring)
  150. What are the three types of pyrimidines?
    Cytosine (C), Thymine (T), and Uracil (U)
  151. What are the two types of purines?
    Adenine (A) and Guanine (G)
  152. What is the chemical formula for phosphate?
  153. What carbon of the sugar does the nitrogenous base attach to in DNA?
    Carbon 1
  154. What carbon of the sugar does the phosphate attach to in DNA?
    Carbon 5
  155. The nitrogenous base uracil (U) is only present in what?
  156. True or False: Bases join adjacent nucleotides on the same DNA polymer.
  157. What is the structure of DNA?
    Double Helix
  158. What are the 3 types of RNA?
    Transfer, ribosomal, and messenger
  159. True or False: The Phosphate-Sugar backbone faces the inside of DNA.
  160. In DNA Adenine (A) pairs with

    A) Cytosine (C)
    B) Uracil (U)
    C) Guanine (G)
    D) Thymine (T)
    D) Thymine (T)
    (this multiple choice question has been scrambled)
  161. In DNA Cytosine (C) pairs with

    A) Thymine (T)
    B) Guanine (G)
    C) Adenine (A)
    D) Uracil (U)
    B) Guanine (G)
    (this multiple choice question has been scrambled)
  162. What does the order of bases do in the sense strand of DNA?
    Carries the genetic code
  163. What does the order of bases do in the antisense strand of DNA?
    Act as a placeholder
  164. Uracil (U) is a substitute for what nitrogenous base in RNA?
    Thymine (T)
  165. In RNA Uracil (U) pairs with

    A) Thymine (T)
    B) Guanine (G)
    C) Cytosine (C)
    D) Adenine (A)
    D) Adenine (A)
    (this multiple choice question has been scrambled)
  166. Where is mRNA formed?
    In the nucleus from a DNA template
  167. What is the structure of mRNA?
    single stranded
  168. What is the purpose of mRNA?
    Caries the code for a specific amino acid sequence in the order of nucleotides

    Moves to cytoplasm to act as a “template” for producing and amino acid sequence
  169. What is a transcription of the DNA nucleotide sequence?
    Messenger RNA (mRNA)
  170. What is the structure of tRNA?
    single stranded
  171. What is the purpose of tRNA?
    Carries specific amino acids for assembly into a protein
  172. What are ribosomes?
    organelles that are the site of protein synthesis
  173. What is the purpose of rRNA?
    Use m-RNA and t-RNA to create the specific amino acid sequence of a protein
  174. How many possible codons are there?
    43 = 64 codons
  175. What is a codon?
    A possible sequence of 3 nucleotides
  176. What are the 4 steps of protein production?
    • Step 1: DNA Template
    • Step 2: DNA as read from 5' to 3'
    • Step 3: mRNA as read from 5' to 3'
    • Step 4: Encoded amino acids

Card Set Information

Eng Bio Macromolecules of Life Notes
2015-01-21 19:15:46
eng bio macromolecules life note exam1 prep

Exam 1 Prep. Second note set.
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