biochem lec chap 4 (MGA NEED I MEMO)

  1. 4-hydroxyproline and 5-hydroxylysine
    Constituents of the fibrous protein collagen, the most abundant protein in mammals
  2. Constituents of the fibrous protein collagen, the most abundant protein in mammals
    4-hydroxyproline and 5-hydroxylysine
  3. y-carboxyglutamic acid
    Constituent of proteins involved in blood clotting
  4. Constituent of proteins involved in blood clotting
    y-carboxyglutamic acid
  5. O-phosphoserine
    Presence of P regulates protein activity
  6. Presence of P regulates protein activity
    O-phosphoserine
  7. cystine
    two cysteine molecules joined by a disulfide bond that plays a role int he structures of many proteins (hair) by forming covalent cross-links
  8. two cysteine molecules joined by a disulfide bond that plays a role int he structures of many proteins (hair) by forming covalent cross-links
    cystine
  9. Ornithine and Citrulline
    Metabolites of the urea cycle
  10. Metabolites of the urea cycle
    Ornithine and Citrulline
  11. Substances having dual (acid-base) nature
    Ampholytes
  12. Ampholytes
    Substances having dual (acid-base) nature
  13. An amino acid polymer of short chain length
    Peptide
  14. Peptide
    An amino acid polymer of short chain length
  15. Polypeptide
    An amino acid polymer of intermediate chain length containing up to 50 amino acid residues
  16. An amino acid polymer of intermediate chain length containing up to 50 amino acid residues
    Polypeptide
  17. Protein
    An amino acid polymer made up of more than 50 amino acids
  18. An amino acid polymer made up of more than 50 amino acids
    Protein
  19. Amino acid residue
    An amino acid that is a part of a peptide, polypeptide, or protein chain
  20. An amino acid that is a part of a peptide, polypeptide, or protein chain
    Amino acid residue
  21. N-terminal residue
    An amino acid on the end of a chain that has an unreacted or free amino group
  22. An amino acid on the end of a chain that has an unreacted or free amino group
    N-terminal residue
  23. C-terminal residue
    An amino acid on the end of a chain that has an unreacted or free carboxylate group
  24. An amino acid on the end of a chain that has an unreacted or free carboxylate group
    C-terminal residue
  25. Glutathione (y-glutamyl-L-cysteinylglycine)
    Protects cells from the destructive effects of oxidation by reacting with substances such as peroxides.
  26. Protects cells from the destructive effects of oxidation by reacting with substances such as peroxides.
    Glutathione (y-glutamyl-L-cysteinylglycine)
  27. Glutathione
    An important intracellular reducing agent
  28. An important intracellular reducing agent
    Glutathione
  29. Oxytocin
    Stimulates contraction of uterine muscles during childbirth and the ejection of milk by mammary glands during lactation.
  30. Stimulates contraction of uterine muscles during childbirth and the ejection of milk by mammary glands during lactation.
    Oxytocin
  31. Opioid peptides
    Molecules that relieve pain and produce pleasant sensations
  32. Molecules that relieve pain and produce pleasant sensations
    Opioid peptides
  33. Examples of Opioid peptides
    • Met-enkephalin
    • Leu-enkephalin
  34. Atrial natriuretic factor
    A peptide produced by specialized cells in the heart and the nervous system
  35. A peptide produced by specialized cells in the heart and the nervous system
    Atrial natriuretic factor
  36. Substance P and Bradykinin
    Peptides that stimulate the perception of pain
  37. Peptides that stimulate the perception of pain
    Substance P and Bradykinin
  38. Structural proteins arranged in fibers or sheets that have only one type of secondary structure
    Fibrous proteins
  39. Fibrous proteins composed of antiparallel beta-pleated sheets
    Silk fibroin
  40. A disease of collagen metabolism
    Scurvy
  41. Interactions between the R groups of nonpolar amino acids
    Van der Waals
  42. Interactions between the polar R groups of the polar amino acids
    Hydrogen bonds
  43. Interactions between the R groups of oppositely charged amino acids
    Ionic bonds (Salt bridges)
  44. Why can diving mammals remain submerged for long periods?
    The storage and distribution of oxygen by muscle myoglobin permits diving mammals to remain submerged for long periods.
  45. Proteins that are insoluble in water
    Fibrous proteins
  46. Proteins that function in the cells as enzymes, hormones, and antibodies
    Globular proteins
  47. Classification of proteins by composition (SIMPLE)
    • 1. Albuminoids
    • 2. Albumins
    • 3. Globulins
    • 4. Histones
  48. Examples of Albuminoids
    • 1. Keratin in skin, hair, and nails
    • 2. Collage in Cartilage
  49. Examples of Albumins
    • 1. Egg Albumins
    • 2. Serum Albumins
  50. Examples of Globulins
    Antibodies
  51. Examples of Histones
    Chromatin in Chromosomes
  52. Classification of proteins by composition (Conjugated)
    • 1. Glycoproteins
    • 2. Lipoproteins
    • 3. Metalloproteins
    • 4. Nucleoproteins
    • 5. Phosphoproteins
  53. Examples and Prosthetic group of glycoproteins
    Interferon - Carbohydrates
  54. Examples and Prosthetic group of lipoproteins
    Lipoproteins - Triglycerides, phospholipid, and cholesterol
  55. Examples and Prosthetic group of Metalloproteins
    Hemoglobin - Metal ion
  56. Examples and Prosthetic group of Nucleoproteins
    Ribosomes - Nucleic acids
  57. Examples and Prosthetic group of Phosphoproteins
    Casein - Phosphate
  58. Classification of proteins by function
    • 1. Structural
    • 2. Contractile
    • 3. Transport
    • 4. Hormonal
    • 5. Catalytic
    • 6. Antibodies
    • 7. Storage
  59. Examples and Functions of the Structural classification of protein
    • 1. Collagen - Build tendons and cartilage
    • 2. Keratin - Forms hair, skin, woo, and nails
  60. Examples and Functions of the Contractile classification of protein
    1. Myosin and Actin - Muscle contraction
  61. Examples and Functions of the Transport classification of protein
    • 1. Hemoglobin - Transports oxygen into bloodstream
    • 2. Lipoproteins - Transport lipids through the body fluids
  62. Examples and Functions of the Hormonal classification of protein
    • 1. Insulin - Increases glucose metabolism
    • 2. Growth hormone - Regulates body growth
    • 3. Estradiol - Stimulates female sex characteristics
    • 4. Testosterone - Stimulates male sex characteristics
  63. Examples and Functions of the Catalytic classification of protein
    • 1. Sucrase - Catalyzes hydrolysis of sucrose
    • 2. Trypsin - Catalyzes hydrolysis of protein
    • 3. Dehydrogenase - Converts ethanol to acetaldehyde
  64. Examples and Functions of the Antibodies classification of protein
    1. Immunoglobulins - Recognizes and destroys bacterial or viral antigens
  65. Examples and Functions of the Storage classification of protein
    • 1. Casein - Stores protein as milk
    • 2. Ferritin - Stores iron in liver for the production of red blood cells
  66. What is the breaking of peptide bonds called?
    Hydrolysis
  67. Too much of what will cost the complete breaking of Peptide bonds?
    Acid
  68. Controlled breaking of peptide bonds will cause what?
    Denaturation of milk
  69. The process of unfolding the native conformation of the protein. It is irreversible.
    Denaturation
  70. Occurs as the protein molecules then unfold and become entangled
    Coagulation
  71. Protein in blood that is involved in the clotting reaction
    Fibrinogen
  72. Protein in blood that protects humans from disease
    Immunoglobulins
  73. Protein in blood that carries hydrophobic molecules in the blood
    Albumins
  74. Denature proteins by disrupting hydrogen bonds within the protein
    Organic Solvents
  75. Disrupt hydrophobic interactions, causing the protein chain to unfold
    Detergents
  76. Interferes with salt bridges that result in loss of conformation between amino acid R groups. React with disulfide bonds and acidic amino acids
    Heavy Metals
  77. Stretches a protein until cross-links break forming a solid
    Agitation
  78. Disrupts hydrogen bonds and hydrophobic attractions; can cause coagulation
    Heat
  79. Disrupts salt bridges
    Acids and Bases
  80. Disrupt the weak interactions that maintain protein conformation
    Mechanical stress
  81. Is a disease that occurs when a random N-terminal is turned into a pleated sheet that causes disastrous effects to the brain and the spinal cord.
    Mad cow disease
  82. Mad cow disease is also called?
    Bovine spongiform encephalopathy (BSE)
  83. What is the human variant of mad cow disease?
    Creutzfeldt-Jakob (CJD) disease
  84. Characteristics of the immune system
    • 1. Highly specific
    • 2. Has memory
    • 3. Can recognize "self" from "nonself"
Author
ZDanuco
ID
359811
Card Set
biochem lec chap 4 (MGA NEED I MEMO)
Description
Updated