A & P 3

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    those that contain CARBON (exs: carbs, lipids, proteins, nucleic acids, & adenosine triphosphate
  2. define ISOMER
    same # of atoms of each element, but different arrangements
  3. Carbon always makes how many bonds?
    • hydroxyl
    • sulfhydryl
    • carbonyl
    • carboxyl
    • ester
    • phosphate
    • amino
    • -OH
    • same as in bases
    • found in alcohols and sugars
    • makes organic molecules water-soluble
    • polar and hydrophilic
    • -SH
    • like hydroxyl, but sulfur+hydgrogen
    • important in protein structure
    • polar and hydrophilic
  7. ESTER
    • formed from reaction of acid and alcohol
    • found in fats, oils, also nerve chemical acetylcholine
    • COOC
    • organic acid (H+ easily donated)
    • also written -COOH
    • usually charged (i.e. -COO-) at cellular pH
    • more oxygen present, more water soluble
    • hydrophilic
  9. AMINO
    • acts as base
    • binds H+ to form -NH3+ at cellular pH
    • amino + carboxyl in same molecule is an amino acid
    • amine-anything with Nitrogen
    • NHH
    • found in energy-storing molecules and in nucleic acids (DNA, RNA)
    • hydrophilic
    • ex: ATP (adenosine triphosphate)
    • PO42-
    • carbon and oxygen in double covalent bond
    • found in KETONES, formed when fats are broken down
    • water-loving groups (hydrophilic)
    • polar
    • CO
  12. arrangements that are commonly found in carbon-containing molecules
  13. what are the 4 main kinds of biological molecules?
    • carbohydrates (sugars)
    • lipids (fats)
    • proteins
    • nucleic acids
  14. define and explain CARBOHYDRATES
    • 5 or 6 carbons
    • "watered carbon"
    • always 1 carbon + 1 water (H2O)
    • formula CxH2xOx (ex: C6H12O6)
    • form ring structures by linking carbons 1 and 5 through an O
    • ratio for carbons-hydrongens-oxygen 1:2:1
    • carbs ALWAYS have same # of carbons as water molecules
  15. define and explain LIPIDS (FATS)
    • carbon, hydrogen, and oxygen (more carbon than oxygen)
    • different proportions than carbs- less O2
    • (more O2- increased solubility)
    • hydrophobic or non-polar- tend to repel water
    • used to build cell membranes
    • (made up of amino acids)
    • amino acids always contain carbon, hydrogen, oxygen, and nitrogen
    • some amino acids include sulfur
    • sugar "backbone" plus nitrogenous base
    • nitrogenous base with one or two rings
    • one-ring pyrimidines (uracil, thymine, cytosine)
    • two-ring purines (adenine, guanine)
    • deoxyribose backbone: DNA
    • ribose backbone: RNA
    • *your body makes DNA & RNA
  18. define MONOMER and give them for each of the 4 main kinds of biological molecules
    • single units
    • carbohydrate- monosaccharide (glucose)
    • protein- amino acid (there are 20)
    • nucleic acid- nucleotide
    • lipid- fatty acid
  19. define POLYMER and give them for each of the 4 main kinds of biological molecules
    • result when monomers are bound together in a string or branched structure
    • carbohydrate- polysaccharides
    • protein- polypeptides (after 30, proteins)
    • nucleic acid- DNA & RNA
    • lipid- triglycerides
    • "building" (taking water out and making something)
    • combo of 2 monosaccharides with formation of water molecule
    • ALL 4 main kinds of biological molecules are dependent on fromation of bonds by dehydration synthesis
    • 5 Carbons
    • ribose
    • deoxyribose
    • 6 Carbons
    • glucose
    • fructose
    • galactose
  23. what are the formulas for the disaccharides?
    • glucose+glucose=maltose
    • glucose+galactose=lactose
    • glucose+fructose=sucrose
  24. what are your MONOSACCHARIDES?
    • glucose
    • fructose
    • galactose
    • deoxyribose
    • ribose
  25. DISACCHARIDES are...?
    • combo of 2 monosaccharides by dehydration synthesis- formed when 2 hexoses combine
    • formed when the -OH of one sugar finds the -H of another and combines to form a water molecule (HOH)
    • sucrose (table sugar)- glucose+fructose
    • lactose (milk sugar)- glucose+galactose
    • maltose- glucose+glucose
    • multiple monosaccharides combined by dehyration synthesis
    • exs: ABO blood group markers: glycogen, starch, and cellulose
  27. explain the role of PENTOSE SUGARS in forming nucleic acids
    • hexoses are a food source, pentoses are NOT, rather they are essential for structure of nucleic acids (RNA & DNA)
    • ribose and deoxyribose differ because deoxyribose has 1 less oxygen(that's what gives it its name)
    • ribose-backbone for RNA
    • deoxyribose-backbone for DNA
  28. what are the 3 major HEXOSES and describe them?
    • glucose- (MOST IMPORTANT!) human cells prefer it as an energy source, is the only significant component of "blood sugar"
    • fructose- found in fruit and honey"fruit sugar" (high fructose corn syrup(HFCS) is glucose converted to fructose by enzymes)
    • galactose- found in dairy products and sugar beets
    • they are all found in significant quanitities in the human diet
  29. define HYDROLYSIS
    • "water breaking"
    • opposite of dehydration synthesis, a water molecule is added to sucrose as it is broken into glucose and fructose (what happens inside our cells as table sugar is metabolized in the diet)

    hydrolysis of scrose is catalyzed by an enzyme invertase (aka sucrase)
  30. name the carbohydrate polymers found in plants and describe each
    • polysaccharides(polymers of carbs) long strings of monomers, may be branched or unbranched
    • cellulose- cell walls, NOT digestible (fiber)
    • starch- storage form of glucose(major source of carbs in diet) CAN be digested
  31. name the carb ploymer found in humans and describe
    • polysaccharide in humans- GLYCOGEN
    • major storage form of glucose in humans
    • mostly in the liver and MUSCLE (mostly)
    • easily broken down (hydrolysis) to glucose(used to power cells(carb loading))
  32. give one example of a polysaccharide found as a surface marker (for blood ABO)
    • GLYCOLIPID- combo of lipids(phospholipids) and sugar(carbs) groups
    • these sugars mark specific cell types
    • process: polysaccharide is attached to a lipid molecule (one monosaccharide involved is galactose)
  33. compare and contrast roles of mono, di, and polysaccharides in human biology
    • (poly) CARBS- most important constituent of human diet- can be used for energy under AEROBIC and ANAEROBIC conditions
    • (poly) starch from plants-important carb source
    • cellulose- "fiber" in diet
    • mono and disaccharides are used as sweeteners
  34. show dehydration synthesis and hydrolysis reaction
    • --> dehydration synthesis (building)
    • <-- hydrolysis (breaking)
  35. synthesis of triglycerides (polymers for lipids)
    • fatty acids added to glycerol backbone by dehydration synthesis
    • triglycerides are held together because of Ester linkage
  36. what are the 6 types/forms of lipids in the body?
    • fatty acids
    • triglycerides
    • phospholipids
    • steroids
    • eicosanoids
    • other lipids (fat soluble vitamins & lipoproteins)
  37. explain POLAR vs NON-POLAR
    • polar- charged (+ or - ions) hydrophilic (likes water)
    • non-polar- uncharged (no ions) hydrophobic (hates water)
  38. define and describe FATTY ACIDS
    • building blocks of lipids
    • monomers of lipids
    • each ends in a carboxyl(-COOH) group, which is where the "ACID" part comes in
    • there are saturated and unsaturated (poly and mono) fatty acids
  39. define SATURATED fatty acids
    • "filled" with hydrogen
    • all the carbons are filled, or saturated, with hydrogen atoms
    • in the zigzag pattern of carbon backbone- its straight
    • solid @ room temp (butter)
  40. define UNSATURATED fatty acids
    • "missing" hydrogens
    • when double bonds form between carbon atoms, fewer hydrogens can bond to carbons
    • the double bond puts a "kink" in the regular zigzag patter of carbon backbone
    • monounsaturated= 1 double bond=1 kink
    • polyunsaturated= many double bonds= many kinks (liquid @ room temp-olive oil)
  41. define and describe TRIGLYCERIDES
    • 3 fatty acid chains added to a molecule of glycerol to form triglycerides
    • dont need to be same size or saturation, can be any combo
    • GLYCEROL backbone
  42. define and describe PHOSPHOLIPIDS
    • formed when 2 fatty acid tails (carbon & hydrogen ONLY) are joined by a glycerol molecule to a phosphate-containing "head group"
    • cell membranes are made up of phospholipids
    • head- polar, hydrophilic- choline
    • neck- polar, hydrophilic- phosphate
    • glycerol- backbone
    • tails- non-polar, hydrophobic- fatty acid (carbon & hydrogen ONLY) molecules
  43. define and explain AMPHIPATHIC
    • associated with phospholipids
    • has polar "head" & non-polar "tails"
    • forms lipid bilayers (oreo cookie) found in cell membranes
    • the tails associate (face) with eachother and the heads associate with water
  44. define and explain STEROIDS
    • CHOLESTEROL is the basis for this class of molecules (we CAN'T live without it)
    • exs: vitamin D, estradiol(type of estrogen), testosterone, and cortisol
  45. define and explain EICOSANOIDS
    • PROSTAGLANDINS & LEUKOTRIENES- "local hormones"- affects sight of damage right there
    • prostaglandins & leukotrienes derive from ARACHIDONIC ACID
    • they are key chemicals in immune defense and inflammation
    • leukotrienes contribute to inflammation associated with asthma
    • prostaglandins contribute to pain/inflammation associated with immune response
  46. define and explain FAT-SOLUBLE VITAMINS
    • ADEK
    • vitamin A is synthesized from carotenes- important in vision (signs-poor teeth & gums, night blindness)
    • vitamin D is important in bone formation, cholesterol derivative (sign-rickets (low blood calcium, soft bones, distorted skeleton))
    • vitamin E is a protective molecule (skin protection)
    • vitamin K is important in blood clotting (sign-slow blood clotting)
  47. define and explain LIPOPROTEIN
    • lipid carriers in blood
    • differ in density, have different effects on health
    • lipids are less dense than water (oil floats)
    • VLDL- high lipid content(low protein) Very Low Density Lipoprotein- most damaging form of lipoprotein (BRINGS fats to heart)
    • LDL- intermediate lipid content- Low-Density Lipoprotein
    • HDL- highest protein cotent, lowest lipid content, its believed to exert protective effect, its increased by exercise- High Density Lipoprotein (best one, carries fats AWAY from heart)
  48. name the 2 FUNCTIONAL GROUPS on AMINO ACIDS and explain amino acids a little bit
    • 2 carbons and a nitrogen form backbone (middle)
    • amino group- nitrogen is bonded to 2 hydrogens (on side)
    • carboxyl group- carbon, 2 oxygen, hydrogen (other side)
    • (side chain) R & H
    • AMINO GROUP-NH2 when uncharged, NH3 + when charged (ionized)
    • CARBOXYL GROUP- -COOH when uncharged, -COO- when charged (ionized)
    • (R GROUPS- placeholders)
    • all of that together, with dehydration synthesis form peptide bonds (remember the drawing of amino and carboxyl groups and then removing H2O (dehydration synthesis) to form a peptide bond) the result from that is called a dipeptide and more than 2 amino acids is called a polypeptide
    • enzymes, called peptidases or proteases break peptide bonds by hydrolysis
  49. 20 AMINO ACIDS- what you NEED to know
    • differ in their R groups & have different chemical properties:
    • polar(hydrophilic) vs non-polar(hydrophobic)
    • acidic vs basic
  50. define DISULFIDE BONDS
    • formed from Cysteine, with its -R group containing a sulfhydryl
    • help hold proteins together
  51. simplest amino acid
  52. makes bend in amino acid chain (folds back into itself)
  53. purple box
    CLOWNS- oddballs (unique)
  54. green box
    • GAYS- polar, charged
    • acids (left) & bases (right)
  55. blue box
    BOYS- polar, uncharged- don't share equally
  56. in the thyroid, Iodine is added to what? to make thyroid hormones
  57. pinkish box
    GIRLS- non-polar, share equally
  58. describe protein PRIMARY STRUCTURE and what are the 2 primary sequences?
    • start of a protein structure
    • (the order in which amino acids are strung together) sequence of amino acids forming its polypeptide chains
    • 2 primary sequences: 1-ELVIS(glutamic acid-leucine-valine-isoleucine-serine) 2-ferret beta-actin
  59. which amino acid is always first in every protein?
  60. describe protein SECONDARY STRUCTURE and give examples
    • form a helices(coil)-ex hair(keratin)
    • form pleated sheats(fold)-ex proteins in nature, like spider silk- H bonds and dotted lines
    • amino acids that DON'T have secondary structure are THREADS
  61. describe protein TERTIARY STRUCTURE and examples
    • how helices or sheets are arranged in 3D
    • types of atomic ineractions leading to tertiary structure: 1-ionic bonds 2-hydrophobic interactions 3-Van der Waals interactions
    • 4-disulfide bridges 5-hydrogen bonds
  62. what are the four levels of STRUCTURE?
    • primary
    • secondary
    • tertiary
    • quaternary
  63. describe protein QUATERNARY and examples
    2 or more identical subunits

    *if a change occurs in primary, it will lead to changes in ALL of them
  64. define DENATURATION
    • when we disrupt the interactions between bonds, and unfold a protein, leaving the primary structure intact
    • *it destroys secondary, tertiary, & quaternary structures
  65. what are the 6 types of proteins & their functions?
    • STRUCTURAL-form structural framework of various parts of the body (collagen, keratin)
    • REGULATORY-funtion as hormones that regulate various physiological processes: control growth and development; as neurotransmitters, mediate response of the nervous system (insulin)
    • CONTRACTILE-allow shortening of muscle cells, which produces movement (myosin, actin)
    • IMMUNOLOGICAL-aid responses that protect body against foreign substances and invading pathogens (antibodies, interleukins)
    • TRANSPORT-carry vital substances throughout the body (hemoglobin)
    • CATALYTIC-act as enzymes that regulate biochemical reactions (salivary amylase, sucrase, & ATPase)
  66. define an ENZYME
    • proteins that speed up (catalyze) chemical reactions
    • proteins that are needed in ALL cells
    • they lower the amount of energy needed to start the reaction, but not the overall energy profile
    energy needed to make alignment happen
    • CATALYSTS make reactions go faster, but are NOT CONSUMED
    • the substance undergoing the reaction= SUBSTRATE (TARGET)
    • enzymes are specific (like puzzle pieces)
  69. what are the 3 things about enzymes?
    • 1-speed up
    • 2-specific
    • 3-don't consume (reusable)
  70. what are the bases and sugars in DNA & RNA?
    • DNA- bases: Adenine, Cytosine, Guanine, & Thymine
    • sugar-deoxyribose
    • RNA-bases: Adenine, Cytosine, Guanine, & Uracil
    • sugar-ribose
  71. what are the 3 units/parts of NUCLEOTIDES
    • a base
    • a sugar
    • a phosphate group
  72. what are the PYRIMIDINES?
  73. what are the PURINES?
  74. name the key structural features of DNA
    • consists of 2 twisted strands (double helix)
    • used to transmit genetic information
    • backbone- sugar(deoxyribose) + phosphate

    • always in those pairs:
    • (3 hydrogen bonds)
    • cytosine>(chewing gum) C-G base pair
    • guanine

    • (2 hydrogen bonds)
    • adenine>(apple tree) A-T base pair
    • thymine
    • hydrogen bonds between bases hold strands together
  75. name the key structural features of RNA
    • unstable
    • used for temporary storage & manipulation of genetic info (scratchpad)
    • does NOT form double helices- single strand
    • backbone-sugar(ribose) + phosphate
    • cytosine
    • guanine
    • adenine
    • uracil
  76. explain biological role of ATP (adenosine triphosphate) and how it's used to produce cellular energy
    • energy currency
    • in a subcellular compartment (mitochondrion), oxygen & glucose are converted cellular energy, which is then stored as high-energy phosphate bonds in a molecule(ATP)
  77. what are the 5 forms of CELLULAR ENERGY?
    • ELECTRICAL- nerve impulses
    • HEAT- cellular chemical reactions
    • MECHANICAL- muscle contractions
    • POTENTIAL(chemical)- energy-rich covalent bonds
    • RADIANT- photosynthesis in plants
  78. define and explain WATER SOLUBLE VITAMINS
    • VITAMIN C- collagen synthesis in connective tissues (signs scurvy (bleeding gums, loose teeth, swollen joints; slow wound healing; weight loss))
  79. explain vitamins as cofactors in enzymatic reactions
    need vitamins to assist or work with enzymes to facilitate better work
  80. give element, function, & human deficiency signs of MINERALS
    • FLUORINE- structure of teeth/bones, effect on cells which build or break down bone; inhibits microorganisms which degrade teeth(signs-increased incidence of dental caries; osteoporosis)
    • CHROMIUM- efficient use of insulin(signs-relative insulin resistance; impaired glucose tolerance; elevated serum lipids)
    • IRON- oxygen & electron transport; heme group of hemoglobin(signs-anemia)
    • IODINE- constituent of thyroid hormones(signs-goiter; depression of thyroid function; (if congenital) cretinism)
Card Set
A & P 3
The Molecular Level of Organization
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