A&P Chapter 2 - Biochemistry

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tiffanydawnn
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A&P Chapter 2 - Biochemistry
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2011-02-03 12:47:34
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A&P Chapter 2 - Biochemistry
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  1. biochemistry
    study of organic molecules
  2. CHNOPS
    • all have CH
    • most have NO
    • some have PS
  3. 5 types of organic molecules
    • carbohydrates
    • lipids
    • proteins
    • nucleic acids
    • ATP
  4. catabolism
    • aka hydrolysis
    • complex macromolecules break down into simple components
    • water added
    • ABCD + H2O -> A+B+C+D
  5. anabolism
    • aka dehydration synthesis
    • simple molecules recombine to form complex macromolecules
    • water removed
    • A+B+C+D -> ABCD + H2O
  6. carbohydrates
    • simple sugars, starches, glycogen, cellulose
    • all contain CHO (1:2:1 ratio)
    • most end in -ose
    • easily metabolized by the body
    • provide most energy used by the body
    • 3 classes: monosaccharides, disaccharides, polysaccharides
  7. monosaccharides
    • simplest sugars
    • 3-7 carbons
    • triose, tetrose, pentose, hexose, heptose
  8. *pentose*
    • C5-H10-O5
    • forms isomers deoxyribose and ribose
  9. *hexose*
    • C6-H12-O6
    • forms isomers glucose, fructose, galactose
  10. disaccharides
    • 2 monosaccharides joined anabolically
    • maltose, sucrose, lactose
  11. maltose
    glucose + glucose
  12. sucrose
    glucose + fructose
  13. lactose
    glucose + galactose
  14. polysaccharides
    10-100 monosaccharides joined anabolically
  15. *glycogen*
    • many glucose molecules recombined anabolically
    • only stored in liver and skeletal muscle cells until needed
  16. cellulose
    • plant starch aka fiber
    • no nutritional value
    • required for proper digestion
  17. lipids
    • 18-25% of body weight in lean adult
    • contain CHO (no 1:2:1 ration - less O2)
    • mostly hydrophobic (do not dissolve in water)
    • dissolve in alcohol, ether, chloroform, xylene, mineral spirits, other lipids
    • contain 2x energy of carbs or protein
    • energy is not efficient b/c fats are difficult to breakdwon
    • unlimited ability to store fats (lots of adipocytes)
    • excess carbs/proteins converted to fat and stored
    • 4 classes: triglycerides, phospholipids, steroids, eicosanoids
  18. triglycerides
    • most abundant lipid
    • solid (wax) or liquid (oil) at room temp
    • always form fatty acid + glycerol when broken down
  19. phospholipids
    • lipid found in cell membranes
    • ampiphathic - polar (react w/water) head/non-polar (react w/ other lipids) tail
  20. steroids
    • lipid with unique 4 carbon ring structure
    • 4 types: testosterone/estrogen, vitamin D, cholesterol, bile salts
  21. testosterone/estrogen
    • steroid
    • sex hormone
    • secondary sex characteristics
  22. vitamin D
    • steroid
    • made in skin
    • for bone development
  23. cholesterol
    • steroid in cell membranes
    • necessary for vitamin D
  24. bile salts
    • steroid
    • breaks down fats during digestion
  25. eicosanoids
    • 20 carbon fatty acid (arachiadonic acid)
    • 2 types: prostaglandins, leukotrinnes
  26. prostaglandin
    • eicosanoid
    • regulate temp
    • keep air passages open
    • clot blood
    • prevent ulcers
    • determine response to hormones
  27. leukotrinne
    • eicosanoid
    • helps control allergic and inflammatory responses
  28. *proteins*
    • contain CHNO sometimes S
    • complex, wide variety of functions
    • **chain of amino acids joined by peptide bonds**
    • various shape depending on protein
    • 4 structures: primary, secondary, tertiary, quaternary
    • 5 functions: contractile, structural, catalytic, immunological, transport
  29. primary protein structure
    long, linear, one-dimensional protein
  30. secondary protein structure
    primary protein folds into pleated sheets or coils into a helix
  31. tertiary protein structure
    • protein folds back on itself
    • AAs originally on opposite ends are next to each other
  32. quaternary protein structure
    2 or more protein chains twist together
  33. contractile protein
    proteins that shorten (ex. actin/myosin)
  34. structural protein
    proteins that form structures (ex. collagen)
  35. catalytic proteins
    enzymes that speed up reactions n the body
  36. immunological proteins
    antibodies
  37. transport proteins
    ex. hemoglobin
  38. *denature*
    when an S, Q, or T protein stops functioning after it encounters a hostile environment (ex. excessive heat or acid)
  39. enzymes
    • unique proteins that speed up chemical reactions
    • most end in -ase
  40. holoenzyme
    a complete enzyme
  41. apoenzyme
    protein portion of an enxyme
  42. co-enzyme
    organic non-protien portion of an enzyme
  43. co-factor
    metallic non-protein portion of an enzyme
  44. *substrates*
    • specific molecules in the body that enzymes are programmed to seek out
    • each enzyme has a unique substrate
  45. active site
    • reigon on enzyme where it combines with substrate
    • induced fit: combines like lock and key
    • reactions occur and products are produced
    • products move away from site of reaction
    • enzyme and substrade split
    • enzyme is free to cause another reaction
  46. nucleic acids
    • largest molecules in the body
    • CHNOP
  47. nucleotide
    • basic structure of nucleic acid
    • pentose sugar (C5): deoxyribose or ribose
    • phosphate group: forms backbone of NA
    • nitrogenous bases: Adenine, Guanine, Cytosine, Thymine, Uracil
  48. DNA
    • always in the nucleus (never leaves)
    • contains heredity info for entire organism, instructions for making every protein in the body
    • double stranded - twisted into double helix
    • pentose sugar is deoxyribose
    • bases are A G C T
    • A = T
    • G = C
    • paired bases joined by hydrogen bonds
  49. RNA
    • found in nucleus and cytoplasm
    • carries out DNA instructions for making protien
    • single stranded - linear or folded
    • pentose sugar is ribose
    • bases are A G C U
    • A = U
    • G = C
    • paired bases joined by hydrogen bonds
    • 3 types: mRNA, rRNA, tRNA
  50. mRNA
    • messenger RNA
    • copy of DNA that takes genetic code to ribosome
  51. rRNA
    • ribosomal RNA
    • small part of ribosome that reads mRNA
  52. tRNA
    • transfer RNA
    • attaches to amino acids in cytoplasm
    • brings AAs into ribosome to make protein when signaled
  53. protein synthesis
    • how proteins are made
    • 2 steps: transcription and translation
    • DNA contains blueprint
    • 20 different amino acids
    • most proteins contain 100 - 1000 AAs
    • **number, type, and order of AAs determine specific protein**
    • each AA is coded by 3 nitrogen bases
    • unique codons on mRNA determine when protein synthesis starts/stop
  54. triplets
    3 nitrogen bases on DNA
  55. codons
    3 nitrogen bases on mRNA
  56. anticodons
    3 nitrogen bases on tRNA
  57. initiator/start codon
    • AUG
    • when ribosome reads it, protein synthesis begins
  58. stop codon
    • UAA, UAG, UGA
    • when any one is read, protein synthesis stops
  59. transcription
    • 1st step in protein synthesis
    • occurs in the nucleus
    • geneitic code in DNA is copied to mRNA
    • initiated by RNA polymerase - enzyme that initiates transcription
    • --attaches to DNA
    • --causes it to uncoil
    • --breaks hydrogen bonds between DNAs nitrogen bases
    • --separates into 2 strands - sense strand and antisense strand
    • as it reads, it copies entire sense strand to a strand of mRNA
    • SNURPS remove introns and splice exons together
    • mRNA (exons) leaves nucleus and travel to ribosome
    • sense/antisense strands re-coil into helix
  60. sense strand
    strand of DNA that RNA polymerase reads
  61. antisense strand
    strand of DNA that RNA polymerase does not read
  62. exon
    info on the sense strand that is used to code for protein
  63. intron
    info on the sense strand that is NOT used to code for protein
  64. translation
    • 2nd step in protein synthesis
    • occurs in cytoplasm at ribosome
    • genetic code in mRNA is transferred to a protein
    • 3 steps: initiation, elongation, termination
  65. initiation
    • mRNA reaches ribosome
    • attaches to rRNA
    • rRNA reads codons
    • when AUG is read, large and small ribosomal subunits lock together over mRNA
    • 1st tRNA and its AA enter P-site
    • codon and anticodon bind - initiation complete
    • 1st AA is always methionine
  66. elongation
    • lengthening of AA chain
    • code in mRNA is translated to a protein
    • 2nd tRNA/AA enter A site (amino acid site)
    • peptide bond forms between AA1 and AA2
    • codon and anticodon bind, filling ribosome
    • ribosome slides to next codon
    • 1st tRNA/AA now in cytoplasm
    • hydrogen bond between 1st tRNA/AA breaks
    • 2nd tRNA/AA slide from A site to P site
    • A site empty
    • process repeats
  67. termination
    • when rRNA reads stop codon
    • UAA, UAG, UGA (any one)
    • release factor enzyme activated - splits ribosome back into 2 subunits and cuts protein away
  68. ATP
    • preferred source of energy required by the body
    • obtained from sugar, AAs, fatty acids, glycerol
    • produced in the mitochondria

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