Untitled

 

  • fjdsh
    • fdsjkhfjk
    • fsdjahf
    • fjdhsakf
      • fjhdsakf
  • fsdjkahfkas
    • dsfjh
    • fejkhf
    • dfjdsfsaf
    • asdfjksdf
    • asdfh

fdshjfjksdkfjsdhjkf hjkfs hfsajkfd hkajhfjkd fdsfsadf

fsafdsjkfh djsk sdajk hjksahdj kfjhksd \n fhjkadshfjkfdhaskf

fjdkshajfksdjkfhjsadhfjklfdsafasdsdfsdfsd

fdsafdsfsdfsdfsdfsdfsdf:

  • \
  • CHNOPS - most common elements in all living matter hdasjkhf jkdhf jkhdksfhjksadh djks fhjksdhjk fsdh jkfahsdjk ah
  • fjdshafasldkjf
  • dsfhsjkdafsdjkhfjkdskjaf dhkj
  • fdsjka
  • **fdsafhdsjfjshdfjkds:**fdsfdsf
  • **Bello:**fdshajfk
  • Bonds
    • ionic bonds: transfer electrons
    • covalent bonds: sharing- polar/unequal sharing and non-polar/equal sharing
    • hydrogen: weak bonds between hydrogen and negatively charged items
    • hydrophobic interactions: how non-polar compounds congregate together- lipids
  • pH
    • acid-base/ 0-14, # of H ions determines scale; logarithmic- pH 3 = 10-3 = 1/1000
    • blood- 7.4, stomach- 2, small intestine- 8; enzymes are specific to pH
  • Water properties
    • polarity
    • cohesion: attraction to other water molecules
    • adhesion: attraction to other charged compounds
    • low density when frozen
    • versatile solvent
    • high heat of fusion/vaporization
    • surface tension
  • Organic molecules - monomers are simplest form of all; monomers join together via dehydration synthesis (loss of water) to make polymers; polymers are broken down via hydrolysis (input of water)
    • Carbohydrates- CHO 1:2:1 ratio, monomer= monosaccharides, 2=disaccharides, 3 or more= polysaccharides
    • Used for energy (cell respiration)
    • Examples
      • glucose- immediate energy to make ATP
      • starch- stored energy in plants
      • glycogen- stored energy in animals (stored in liver)
      • cellulose- plant cell wall
      • Lipids – C, H, O (not a 1:2:1 ratio) *P only in phospholipids (1) fats, waxes, oils and sterols (2) Saturated fats have single bonds between carbons, unsaturated fats have at least one double bond between carbons (kinky); plants make polyunsaturated; animals make monounsaturated (3) Phospholipids make up cell membranes (double layer) and are amphipathic- hydrophilic and hydrophobic (4) Uses- in all membranes; stored energy, protection, insulation, myelin sheath of nerves c. Proteins- C, H, O, N (may have other elements in R group) (1) Monomer- amino acids (20 total types), 2=dipeptide, 3 or more= polypeptide (2) Parts of amino acid= carboxyl group (COOH) on one end, amino group on the other end (NH2), central carbon and variable R group (can be hydrophobic or hydrophilic) which determines chemical properties. (3) Protein Folding- shape determines function; primary= a.a. chain; secondary= beta pleated sheet or alpha helix( hydrogen bonds); tertiary=globular; folds in on itself (disulfide bridges, hydrogen bonds, hydrophobic interactions; ionic bonding); quartenary= more than one polypeptide. (4) Uses- protein carriers in cell membrane, antibodies, hemoglobin, enzymes, most hormones� Page 3 AP Biology: 2013 Exam Review d. Nucleic acids – C, H, O, N (1) Monomer= nucleotide, 2 = dinucleotide, 2 or more polynucleotide (2) Nucleotide made up of sugar, phosphate and base (3) Used to store genetic information (4) DNA is double stranded, has deoxyribose, A, G, C, T (5) RNA is single stranded, has ribose, A, G, C, U (6) mRNA- copies genetic message; rRNA- attaches mRNA and makes up ribosomes (most common);tRNA- carries amino acids; DNA- carries genetic code
  • Enzymes a. Biological catalysts (made of protein) that speed up rate of chemical reactions by lowering activation energy required for reaction to occur b. Enzyme has active site (exposed R groups) where reaction occurs c. Enzymes can break down substance (catabolic reaction) or build up substances (anabolic) d. Enzyme/substrate complex is formed e. Substrate is what enzyme acts on f. Rate is determined by collisions between substrate and enzyme g. Ends in –ase, named after substrate often h. Enzyme is specific to substrate; the substrate must be complementary to the surface properties (shape and charge) of the active site (which is made up of R groups with specific chemistry, i.e. hydrophobic). i. Enzyme rate is affected by:  pH (optimal for each enzyme),  temperature (optimal for each enzyme but in general increased temp means increased collisions so rate goes up initially; too much heat can denature enzyme), enzyme concentration (more enzyme faster rate or vice versa)  substrate concentration (more substrate faster rate; vmax is fastest enzyme can work when saturated) j. Inhibition-competitive inhibition (something competes for active site; can be overcome with more substrate) k. Non-competitive inhibition- attaches at allosteric site and changes shape of enzyme so it is not functional; can not be overcome with more substrate l. Coenzymes (organic; NAD and vitamin B etc.) and cofactors (inorganic; zinc, magnesium etc.) interact with enzymes to put them into the right structure to do work.