Bio SAT: Chapter 3

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swbell14  on May 23, 2011

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bio sat

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Bio SAT: Chapter 3

at the elemental level, all life is composed primarily of...
carbon, hydrogen, oxygen, nitrogen, phosphorous, and sulfur or CHNOPS
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at the elemental level, all life is composed primarily of... carbon, hydrogen, oxygen, nitrogen, phosphorous, and sulfur or CHNOPS
inorganic compounds do not contain carbon
organic compounds include carbon
polar covalent water; has a positively charged side and a negatively charged side; since the molecule is bent its unequal charge distribution makes one end positive and the other end negative
covalent atoms share electrons
dipole moment unequal distribution of charge
hydrogen bonds partial positive and negative charges of water attract each other
more heat= more rapid movement of molecules
liquid hydrocarbons very low boiling points because molecules are held together very weakly
ice is less _____ than water dense
ice being less dense than water allows it to... float on top of water and prevent layers of water beneath it from freezing
true or false? water molecules are charged false
dipole-dipole interactions interactions that water can form with sugar molecules, displacing their interactions with each other and allowing the molecules to leave the crystal to float surrounded by water molecules
solvent substance that does the dissolving
solute molecules that are dissolved
molarity the number of moles of solute in one liter
acid proton donor
base proton acceptor
proton H+; hydrogen atom stripped of its single electron, leaving a positively charged proton
HCI--> H+ + CI-
Water as an acid H2O-->H+ + OH-
Water as a base H+ + H2O-->H3O+
hydrocarbon chain basic backbone of organic molecules; upon which functional groups are found
hydroxyl (OH) contained in polar compounds such as alcohols and carbohydrates; polar; increases water solubility; involved in hydrogen bonds
carbonyl (C=O) polar; double bond between C and O contained in aldehydes and ketons, including formaldehyde
Carboxyl (COOH) polar groups; contained in carboxylic acids; lose H+ ions to form acids like vinegar; have negative charge when lose proton; in fatty acids and amino acids
Amino (NH2) polar; found in methylamine and amino acids; can be primary, secondary, or tertiary; can act as bases; primary become positively charged when protonated in molecules like amino acids;
carbohydrates/sugars/saccharides functions: important roles in engery metabolism and store, and structure of cell and organism; C:H:O=1:2:1
cellulose provides cell wall of plants; single most abundant biological molecule on earth
monosaccharides simple sugars; glucose and fructose; CHO 121;
disaccharides sugars with two monomers
polysacharides sugars with lots of monomers; glycogen, starch, and cellulose; carbohydrates formed by joining many monosaccarides together into large ploymers
stereochemistry...
chiral carbons a carbon with four nonequivalent groups attached; make sugars optically active
glycosidic linkages covalent bonds formed between simple sugars
maltose disaccharide formed by joining two glucose molecules together
dehydration reaction reaction to form the disaccharide; water molecule is removed in the process
hydrolysis reaction to form two glucose molecules from a single maltose; addition of a water molecule
sucrose common table sugar; made of a glucose molecule and a fructose molecule joined together
Lipids (fats and oils very nonpolar; tend to repel water; play important roles in energy metabolism and in cellular membranes; CHO; long-term energy storage in animals
triglycerides lipids used by animals to store energy
fatty acids...
ester linkages...
glycerol...
phospholipidslipid molecules with polar phosphate-containing "heads" on one end and nonpolar fatty acid "tails" on the other end; when mixed with water, will spontaneously form structures with the fatty acids gather together to keep out water and the phosphate group pointing out toward water; glycerol, two fatty acids; phosphate group, lecithin
lecithing a nitrogen-containing alcohol; major constituent of lipid bilayer cell membranes
waxes esters of fatty acids and alcohols; form protective coatings
steroids three fused cyclohexane rings and one fused cyclopentane ring
cartotenoids conjugated double bonds and carry six-membered carbon rings at each end; pigments; produce red, yellow, orange, and brown colors in blants and animals; carotnes and xanthophylls
proteins provide cells with the ability to carry out many functions; polymers formed by joining amino acids together during translation
peptide bonds how amino acids are joined together in a chain
polypeptide string of amino acids
protein folding process by which bonds in the ploypeptide flexibly rotate and allow the amino acids in the polypeptide chain to fold flexibly in many different ways; determined by the order and identity of the amino acids
four levels of protein structure primary, secondary, tertiary, quaternary
primary level of protein structure sequence of the amino acids joined together in the linear polypeptide chain
secondary level of protein structure includes regular repeating elements of folding that involve interactions between functional groups of local neighbors in the polypeptide
tertiary level of structure folding due to boding between side chains of the various amino acids
quaternary level of protein structure results from interactions between different polypeptides to form a single functional unit
enzymes biological catalysts to speed up reactions and make them useful for living organisms
substrates reactants in enzymatic reactions
transition state unstable high-energy state which chemicals must pass through to become products
activation energy amount of energy required to reach the transition state
active site three-dimensional binding pocket contained in the folded polypeptide; in which reaction is catalyzed; contain specific amino acids precisely oriented in the protein's structure to form a substrate binding pocket
enzyme activity amount of catalysis by an enzyme
saturability at a certain point, adding more reactants faster will not produce products faster only in enzyme-catalyzed reactions
V max maximal reaction rate observed with the saturated enzyme
specificity to fit in the active site and be used as a substrate, a chemical must have the specific shape of the substrate that the enzyme recognizes, determined by the precise orientation of amino acids in the binding pocket

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