Terms : Hide Images
| 12122318973 | hydrogen bonding | interaction between molecules with O, H, N, F, or Cl | 0 | |
| 12122330012 | polar | electrons shared unequally (ex water, forms hydrogen bonds with other polar molecules) | 1 | |
| 12122343813 | solid water | ice, moderate density | 2 | |
| 12122347641 | liquid water | highest density | 3 | |
| 12122350370 | gas water | steam, lowest density | 4 | |
| 12122360609 | benefits of polarity | can dissolve polar molecules, immiscible with membranes and other nonpolar structures | 5 | |
| 12122370973 | benefits of hydrogen bonds | high boiling point and heat capacity, low density of ice, adhesion and cohesion, surface tension | 6 | |
| 12122380596 | dissociation of water | H₂O ⇌ H⁺ ₊ OH⁻ or 2H₂O →H₃O⁺ ₊ OH⁻ | 7 | |
| 12122410684 | pH | -log[H⁺], <7 = acidic, >7 = basic | 8 | |
| 12122420312 | pOH | = -log[OH⁻] | 9 | |
| 12122430208 | carbon | makes four covalent bonds in chains, which can be bent, straight, or branched; forms macromolecules | 10 | |
| 12122437563 | dehydration synthesis | removing water to link a monomer to a polymer chain, occurs between: - OH and OH in carbohydrates - NH₂ and COOH in proteins - COOH and OH in lipids | 11 | |
| 12122481091 | carbohydrates (visual) |  | 12 | |
| 12122493882 | carbohydrate monomer | monosaccharide | 13 | |
| 12122496032 | carbohydrate polymer | polysaccharide | 14 | |
| 12122500298 | carbohydrate basic formula | CH2O | 15 | |
| 12122504698 | carbohydrate bond | glycosidic linkage (covalent bonds) | 16 | |
| 12122512533 | carbohydrate functions | - starch: storage in plants (digestable) - cellulose: storage in plants (indigestable) - glycogen: storage in humans (liver) | 17 | |
| 12122533831 | fatty acid (visual) |  | 18 | |
| 12122539437 | triglyceride (visual) |  | 19 | |
| 12122543690 | steroid (visual) |  | 20 | |
| 12122550738 | phospholipid (visual) |  | 21 | |
| 12122556828 | lipid monomer | fatty acid | 22 | |
| 12122560874 | lipid bond | ester linkage | 23 | |
| 12122564145 | fat | glycerol and three fatty acids | 24 | |
| 12122572536 | phospholipids | - phosphate group and two fatty acids - aggregate spontaneously in water - form micelles and bilayers with nonpolar, hydrophobic tails inside and polar, hydrophilic heads outside | 25 | |
| 12122599885 | steroid | lipid with four fused rings | 26 | |
| 12122603966 | cholesterol | type of steroid, helps membranes stay fluid | 27 | |
| 12122611127 | lipid functions | store energy, make up cell membranes, hormones | 28 | |
| 12122617756 | saturated fat | saturated with hydrogens, all single bonds, compressible | 29 | |
| 12122624114 | unsaturated fat | double bonds, not compressible | 30 | |
| 12122633117 | nucleic acid (visual) |  | 31 | |
| 12122640829 | nucleic acid monomer | nucleotide | 32 | |
| 12122640830 | nucleic acid polymer | polynucleotide | 33 | |
| 12122646169 | nucleic acid bond | phosphodiester linkage | 34 | |
| 12122649590 | nucleic acid structure | sugar phosphate backbone and nitrogenous base | 35 | |
| 12122670453 | nucleic acid types | - ribose - deoxiribose - no O on 2nd carbon (carbons counted from attachment point of nitrogenous base) | 36 | |
| 12122682339 | nucleic acid functions | DNA directs RNA synthesis, stores hereditary info RNA directs protein synthesis, codes for cell activities | 37 | |
| 12122707710 | protein (visual) |  | 38 | |
| 12122715310 | protein monomer | amino acid (peptide) | 39 | |
| 12122718587 | protein polymer | polypeptide | 40 | |
| 12122718588 | protein bond | peptide bond | 41 | |
| 12122721136 | R group in proteins | differs for each amono acid | 42 | |
| 12122728140 | protein function | accelerate chemical reactions, provide structure and support, transport substances, coordinate organism activity (hormones), movement, cell response to stimuli, protect against disease, enzymes *shape determines function* | 43 | |
| 12122755449 | protein structure | determined by amino acid sequence and the way in which it folds due to the environment it's in | 44 | |
| 12122762103 | protein primary structure | chain of amino acids with a unique order | 45 | |
| 12122769384 | protein secondary structure | alpha helix and beta pleated sheets (folds in peptide chain) held together by hydrogen bonds | 46 | |
| 12122810759 | protein tertiary structure | 3D folding, overall sructure held together by disulfide bridges, ionic bonds, hydrogen bonds, Van der Walls forces | 47 | |
| 12122833568 | protein quaternary structure | assembly of tertiary subunits (not in all proteins) | 48 | |
| 12122848339 | protein denaturation | when a protein loses its 3D shape due to pH, temp, salinity, etc (environmental factors) - sometimes reversible, sometimes not | 49 | |
| 12122872369 | cell membrane | creates food vacuoles, allows intercellular communication, contains identity proteins and Na+/K+ pumps, recycles/reuses cell membrane components | 50 | |
| 12122886852 | cell wall | prevents cell from bursting in hypotonic environments (not in animals) | 51 | |
| 12122933102 | centriole/centrosome | produce spindle fibers during cell division (animals only) | 52 | |
| 12122936577 | chloroplasts | light and dark reactions of photosynthesis, near cell membrane (plants only) | 53 | |
| 12122950842 | rough ER | recycles/reuses cell membrane components, holds ribosomes, modifies proteins | 54 | |
| 12122965161 | smooth ER | manufactures lipids, recycles membrane components | 55 | |
| 12122971237 | flagella | cellular motility (not in plants) | 56 | |
| 12122976379 | golgi apparatus | modifies and packages proteins into vesicles, peroxisomes, and lysosomes; near ER and membrane for fast transport, reuses cell membrane components | 57 | |
| 12123007844 | lysosome | contains digestive enzymes, merges with food vacuole (not in plants) | 58 | |
| 12123020011 | mitochondria | aerobic respiration | 59 | |
| 12123027067 | nuclear envelope | contains DNA and allows exit of mRNA | 60 | |
| 12123096433 | nuclear pore | allows exit of mRNA | 61 | |
| 12123100204 | nucleolus | makes ribosomal subunits from proteins, ribosomal mRNA | 62 | |
| 12123123656 | peroxisome | contains enzymes that detoxify metabolic waste | 63 | |
| 12123139210 | plasmodesmata | allows intercellular communication (plants only) | 64 | |
| 12123148810 | ribosome | makes proteins from amino acids | 65 | |
| 12123161928 | central vacuole | holds water, materials, and wastes; maintains pressure to provide structure and support (plants only) | 66 | |
| 12123182479 | food vacuole | membrane-enclosed food particles in cell | 67 | |
| 12123188935 | vesicle | transports proteins from ER to golgi | 68 | |
| 12123192717 | SA:V ratio | smaller things have greater SA:V ratio => helpful for interacting with outside world, facilitating cell diffusion, getting nutrients in and wastes out - volume determines energy needs | 69 | |
| 12123221450 | semi-permeable | some things can get through, others can't | 70 | |
| 12123225179 | fluid mosaic | membrane = constantly moving structure with proteins embedded in it, polar and non-polar pieces | 71 | |
| 12123241254 | membrane and membrane protein functions | containment, transport, identity, attachment, signal receiving, chemical reaction sites, attachment to cytoskeleton | 72 | |
| 12123254580 | membrane fluidity | lipids held together by hydrophobic interactions, move laterally (fluidity increases as temperature decreases) | 73 | |
| 12123267146 | phospholipid bilayer | containment, transport | 74 | |
| 12123271495 | glycoproteins | identity, allow for cell-cell recognition | 75 | |
| 12123277181 | receptor proteins | receive chemical signals from hormones etc | 76 | |
| 12123326244 | channel proteins | allow certain molecules to pass through membrane | 77 | |
| 12123345222 | integral proteins | pass through membrane | 78 | |
| 12123349139 | peripheral proteins | loosely bound to the surface of the membrane: attachment points, relay signals, etc | 79 | |
| 12123358153 | embedded proteins | pass partway through membrane | 80 | |
| 12123385055 | composition of membranes | all membranes have the same composition, differ only by proportion and types of embedded proteins | 81 | |
| 12123397563 | transport through semi-permeable membrane | passive - some molecules pass through, others excluded based on size, charge, etc. in general: - small, hydrophobic molecules (O2, CO2, steroid hormones) pass through quickly - small hydrophilic molecules (water, glucose), ions pass through slowly | 82 | |
| 12123431154 | transport proteins | (passive/active) - selective channels through membrane, facilitate diffusion - passive: down concentration gradient; ATP required only to make protein, not for transport - active: against concentration gradient, uses ATP | 83 | |
| 12123458623 | ion channel proteins | allow ions to pass through membrane | 84 | |
| 12123470925 | gated ion channel proteins | can be opened/closed by certain stimuli | 85 | |
| 12123474698 | passive transport | spontaneous, no ATP required, down concentration gradient | 86 | |
| 12123479125 | diffusion | molecules spread out into available space due to thermal energy, movement continues until molecules are as evenly distributed as possible - each substance diffuses down its own concentration gradient, unaffected by concentration gradients of other molecules in the system | 87 | |
| 12123511259 | osmosis | diffusion of water down its concentration gradient across a semi-permeable membrane - high [water] -> low [water] -low[solute] -> high [solute] | 88 | |
| 12123542697 | osmoregulation | maintaining balance in different water environments, such as by pumping water in or out of a cell | 89 | |
| 12123560579 | facilitated diffusion | passive transport requiring the use of a channel, often used for polar molecules and ions - proteins specific to substance | 90 | |
| 12123576300 | isotonic solution | equal concentration inside and outside the cell, net movement of water is 0, cell stays the same size | 91 | |
| 12123585336 | hypertonic solution | more particles in solution than in cell, water moves out of cell to dilute surroundings, cell shrinks | 92 | |
| 12123594116 | hypotonic solution | fewer particles in solution than in cell, water moves into cell to dilute internal environment, cell expands | 93 | |
| 12123626814 | water potential | tendency of water to move out of a solution (water moves from high to low water potential) | 94 | |
| 12123669274 | water potential equation | Ψ = Ψs + Ψp, Ψ=-iCRT i = ionization constant = number of pieces C = concentration (M) R = pressure constant (0.0831 Lbar/molK) T = temperature (K, 273+C) | 95 | |
| 12123731876 | Ψs, solute potential | tendency of water to move out of solution due to [solute]; as M goes up, Ψs goes down - Ψs of water is 0, all others negative | 96 | |
| 12123748983 | Ψp, pressure potential | 0 in open container; as Ψp goes up, Ψw goes up | 97 | |
| 12123758396 | proportionality | constant ration between two things | 98 | |
| 12123771306 | active transport | movement against concentration gradient, requires ATP and channel protein | 99 | |
| 12123777661 | sodium-potassium pump | moves 3NA+ out and 2NA+ in when phosphorelated wit use of ATP, which changes protein shape and allows NA+ to bind - sets up electrochemical gradient | 100 | |
| 12123803483 | proton pump | moves H+ out of the cell, maintains electrochemical gradient with charge across membrane | 101 | |
| 12123813241 | cotransport | transport of several molecules indirectly drive by transport of one - ATP used to pump a molecule to one side of membrane, have it do work as it diffuses back, brings another molecule with it - energy spent only on transporting initial molecule | 102 | |
| 12123855281 | secretory vesicles | excrete things from cell | 103 | |
| 12123859479 | exocytosis | removal of materials from cell: vesicles move from golgi/ER, fuse with cell membrane, dump out contents | 104 | |
| 12123869818 | endocytosis | intake of large quantities: membrane pinches into a pocket, seals into a vesicle | 105 | |
| 12123880999 | phagocytosis | intake of large particles in a food vesicle, not specific | 106 | |
| 12123887048 | pinocytosis | intake of nutrient/iron rich liquid, not specific | 107 | |
| 12123894560 | receptor-mediated endocytosis | receptor cells on membrane bind to ligands, pulled into cell (highly secific) - occurs at coated pits | 108 | |
| 12123911825 | coated pits | areas of membrane with coat proteins on the inside and receptors for specific substances on the outside | 109 | |
| 12123920230 | digestion | occurs when vesicle from phago/endocytosis murges with lysosome | 110 | |
| 12123931496 | recycling membrane | - proteins recycled back to membrane source - when vesicle pinches off, membrane inside becomes vesicle outside, returns to inside when it fuses with membrane (retains "sidedness") | 111 | |
| 12123948091 | amino functional group | NH2, basic |  | 112 |
| 12123956236 | phosphate functional group | H2PO4-, acidic | 113 | |
| 12123975975 | carboxyl functional group | COOH, acidic |  | 114 |
