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BMS 110 Unit 1 Ch. 2 Molecules of Life

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  1. 1biological moleculescompounds built in atoms of element carbon; organic compounds
  2. 2four main biological moleculescarbohydrates, lipids, proteins, nucleic acids
  3. 3organic compoundscontain carbon & at least 1 hydrogen atom
  4. 4inorganic compoundsdoesn't have both carbon & hydrogen
    ex: water (H2O)
  5. 5what behavior does carbon have?versatile bonding behavior
  6. 6what is versatile bonding behavior?each carbon atom can share pairs of electrons with as many as 4 other atoms; covalent bonds are fairly stable because carbon atoms share electrons equally
  7. 7angles of covalent bonds produce...shape of organic compounds
  8. 8hydrocarboncarbon backbone with only hydrogen atoms attached to it
  9. 9functional groupsan atom/cluster of atoms that are covalently bonded to carbon
    -kind, arrangement, # determines specific properties such as polarity or acidity
  10. 10two types of reactionscondensation (anabolic)
    hydrolysis (catabolic)
  11. 11condensation reaction2 covalently bonded into larger one
    -building process
    -water as byproduct
    (aka anabolic)
  12. 12hydrolysis reactionmolecule splits into 2 small ones, releasing water
    -breaking down reaction
    -water as substrate
    (aka catabolic)
  13. 13condensation more in detail-enzymes remove a hydroxyl group from 1 molecule & an H atom from another & speed formation of covalent bond between the 2 molecules
    -discared hydrogen & oxygen atoms may from water (called dehydration synthesis)
  14. 14polymerlarge molecule build of 3 or more subunits (monomers)
  15. 15hydrolysis more in detail-enzymes act on particular functional groups & split molecules into 2 or more parts
    -enzymes attach an OH- group & a H atom from water molecule to exposed sites
  16. 163rd type of metabolic reactionrelocating/rearranging functional groups
  17. 17relocating functional groups reaction-one molecule gives up functional group that immediately is attached to another molecule
    -transfer changes structure/function of both molecules involved
    -electrons may also move from molecule to molecule
  18. 18monomers of the biological moleculescarbohydrates - monosaccaharides
    lipids - glycerol + free fatty acids
    proteins - amino acids
    nucleic acids - nucleotides
  19. 19carbohydrates main ideas-consist of carbon, hydrogen, & oxygen in 1:2:1 ratio
    -most abundant & most readily available
    -used for energy; most preferred
  20. 203 major classes of carbohydratesmonosaccharides, oligosaccharides, & polysaccharides
  21. 21monosaccharides-simplest carbohydrate, simplest sugar
    -has at least 2 OH- groups joined to carbon backbone plus an aldehyde or ketone group
    -backbone of 5 or 6 carbons
    -taste sweet & dissolve easily in water
  22. 22main examples of monosaccharidesglucose, fructose, galactose
  23. 23glucose-monosaccharide
    -main source of energy for body cells; has 6C 12H
    -building block for larger carbohydrates
    -parent molecule (precusor) for many compounds like Vitamin C, dervied form sugar monomers
  24. 24oligosaccharides-short chain of 2 or more sugar monomers that are joined by dehydration synthesis
    -disaccharides consist of 2 sugar units
    -proteins/other large molecules often have oligosaccharides attached as side chains
  25. 25main examples of oligosaccharidesraffinose & stachyose
  26. 26main examples of disaccharidessucrose, lactose, & maltose
  27. 27lactose-disaccharide
    -a glucose & a galactose unit
    -milk sugar
  28. 28sucrose-disaccharide
    -most plentiful sugar in nature; simple sugar
    -consists of 1 glucose & 1 fructose unit
    -in fruits, table salt, other plant foods
  29. 29maltose-disaccharide
    -found in alcohol, bread
  30. 30polysaccharides-straight/branched chains of sugar monomers; "complex" carbohydrates
    -often 1000s joined by dehydration synthesis
    -store energy; energy released to cells when sugar is broken down
    -make up most carbohydrates we eat
  31. 31main examples of polysaccharidesstarch, glycogen, cellulose, & chitin
  32. 32cellulose-plants store large amount of glucose in form of cellulose
    -humans don't have digestive enzymes to break down cellulose in whole grains, fruits, vegetables, etc.
    -undigested fiber adds bulk & helps more wastes through lower part of digestive tract
  33. 33many plant derived foods are rich in...starch
  34. 34glycogen-polysaccharide
    one way animals store sugar (in muscles & liver)
    -person's blood sugar decreases, liver cells break down glycogen & release glucose to blood
    -quick source energy
  35. 35lipids main ideas-nonpolar hydrocarbon
    -hydrophobic; dissolves easily in nonpolar substances
    -fats = largest reserve store of energy
  36. 36uses of lipids-store energy
    -signal molecules
    -structural materials
    -phospholipids build cell membrane
  37. 37fats-largest reserve store of energy
    -lipid with glycerol head & 1, 2, or 3 fatty acid tails
    -fatty acid has backbone up to 36 carbons & a carboxyl group (-COOH) at one end
  38. 38saturated fats & examples-solid at room temp
    -fatty acid backbones only have single covalent bonds
    -ex: butter, lard, chicken fat
  39. 39unsaturated fats & examples-liquid at room temp
    -fatty acid backbones have 1 or more double covalent bonds
    -bonds have rigid kinks to prevent from packing tightly
    -some are unhealthy (ex: trans fat)
    -ex: vegetable oils like canola oil, peanut oil, corn oil, olive oil
  40. 40triglycerides-neutral fat; most common & richest source of energy
    -lipid containing 3 fatty acid tails attached to glycerol backbone
    -yield twice as much energy than complex carbohydrates (have more removable electrons than do carbohydrates (energy released when electrons are removed))
    -specialized storage: adipocytes
    -stored as fat droplets in fat-storing tissues
  41. 41examples of triglyceridesbutter, lard, oils, other dietary fats consist mostly of these
  42. 42phospholipids-glycerol backbone, 2 fatty acids tails, hydrophilic "head" with a phosphate group & another polar group
    -main materials of cell membranes which have 2 layers of lipids
    -fatty acid tails = hydrophobic
  43. 43sterols-lipid with no fatty acid tails & a rigid backbone of 4 fused-together carbon rings
    -components of membranes
    -differ in #, position, & type of their functional group
    -associate sterol cholesterol with heart disease
    -precursors of steroid hormones
  44. 44derivatives of cholesterolVitamin D (bone/tooth development), bile salts (fat digestion in small intestine), & steroid hormones (estrogen & testosterone)
  45. 45proteins main ideas-most diverse
    -organic compound built of 1 or more amino acid chains
    -20 kinds of amino acids
    -do work inside/outside cells
    -catalysts, enzymes, tension/torsion, signaling
    -TOOLS of the body
  46. 46enzymesproteins that speed up reactions
  47. 47structural proteinsbuilding blocks of cells & tissues in bones, muscles, etc.
  48. 48types of proteins & functions-transport proteins move substances
    -hormones adjust cell activities
    -others important in body defenses
  49. 49amino acidsmall organic compound (central carbon atom) that consists of...
    1) an amino group (-NH2)
    2) a carboxyl group (-COOH, an acid)
    3) hydrogen atom
    4) R group/side chain (1 or more atoms)
    -1, 2, 3 stay same on all amino acids
    -linked by peptide bonds
  50. 50R groups-radical side chain
    -help determine an amino acid's chemical properties
    -are unique in every amino acid
  51. 51peptide bonds-COVALENT bond that joins amino group of 1 amino acid to carboxyl group of 2nd amino acid
  52. 52dipeptide bondwhen peptide bonds join 2 amino acids together
  53. 53polypeptide chain-when peptide bonds join 3 or more amino acids together
    -each has unique sequence of amino acids
    -DNA determines order in which amino acids are added to chain
  54. 54primary structureparticular sequence of amino acids that make up a protein
  55. 55when amino acids are done assembling into protein, protein...folds into its final shape
  56. 56a protein's final shape determines...its function
  57. 57protein's primary structure streps1) formation of functioning protein
    2) structure emerges as chain twists
    3) its structure changes, hydrogen bonds form between amino acids in different parts of chain
  58. 58what determines a protein's final shape?sequence of amino acids; folding/interacting of amino acids
  59. 59aspects of secondary structure-hydrogen bonding
    -alpha helix
    -beta pleated sheet
  60. 60tertiary structure & example-what makes protein a molecule that can perform a function
    -continued hydrogen bonding
    -disulfide bridges (covalent)
    -tucking away hydrophoic amino acids
    -ex: hollow "barrel" provides a channel through which substances can move in/out of cells
  61. 61quaternary structure & example-proteins built of 2 or more polypeptide chains
    -hydrogen bonds hold chains together
    -ex: hormone insulin & hemoglobin (protein in RBCs - 4 molecules of globin & iron-containing functional group)
  62. 62collagenmost common protein in body
    -elongated, strong, fibrous
  63. 632 types of final shape of proteins & what are they-fibrous = stringy, touch, usually insoluble in water
    -globular = round, usually water soluble
  64. 64lipoproteins-form when certain proteins in blood combine with cholesterol, triglycerides, & phospholipids that were consumed in food
    -lipids are attached
  65. 65glycoproteinsoligosaccharides are attached
    -most proteins found on surface are glycoproteins & they are many of the proteins in blood & cells that secrete (protein hormones)
  66. 66denatured & examplewhen protein/other large molecule loses its normal 3D shape
    -ex: temp or pH exceeds protein's tolerance, hydrogen bonds break, polypeptide chains unwind/change shape, protein no longer functions
  67. 67nucleotidecomposed of...
    1) 1 sugar (ribose or deoxyribose)
    2) at least 1 phosphate group
    3) 1 nitrogen-containing base (adenine, guanine, cytosine, thymine)
  68. 68ribose5-carbon ring structure, 2 oxygen atoms attached to ring
  69. 69deoxyribose5-carbon ring structure, 1 oxygen atom attached to ring
  70. 70ATPadenosine triphosphate; row of 3 phosphate groups attached to sugar
    -links chemical reactions that release energy with other reactions that require energy
    -can transfer a phosphate group to other molecules in cell providing them with energy
  71. 71coenzymes"enzyme helpers"; move hydrogen atoms & electrons from one energy reaction sit to another
  72. 72cAMPcyclic adenosine monophosphate; acts as chemical messenger in & between cells
  73. 73nucleic acidslong single-stranded or double-stranded chain of 4 different nucleotides joined at phosphate groups
  74. 74DNA-nucleotide; deoxyribonucleic acid
    -double-stranded
    -thymine
    -bases: A, T, C, G
  75. 75RNA-nucleotide; ribonucleic acid
    -single-stranded
    -uracil
    -regulates cellular metabolism, produces proteins, governs developmental timing
    -bases: A, U, C, G
  76. 76DNA contains genetic info to...1) build proteins
    2) regulate physiological processes
    3) maintain homeostasis
  77. 77most energy is available in...spurts (it is not a continuous system)

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Der Nutzer hat seine Fachbereichs-Information gelöscht. Karteikarten am BMS 110 Unit 1 Ch. 2 Molecules of Life , erstellt von Gelöschter Nutzer am 19/09/2021.
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  • Erstellt von Makenna Ornes · 17 Sep 2021
  • Kopiert von Makenna Ornes · 19 Sep 2021
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