7269730283 | organic chemistry | study of carbon compounds | 0 | |
7269730284 | hydrocarbons | - organic molecules only consisting of carbon and hydrogen - hydrocarbon chains are hydrophobic due to their non-polar CH bonds - release energy when broken down | ![]() | 1 |
7269844674 | isomers | compounds with the same molecular formula but different structural arrangements and properties | ![]() | 2 |
7269847005 | cistrans isomers | same sequence of covalently bonded atoms but overall differ in structure due to inflexibility of double bonds - cis isomer has same atoms attached to same carbons on one side of double bond - trans has atoms on opposite sides of double bond | ![]() | 3 |
7269857536 | enantiomers | left and right handed versions of a molecule and can differ greatly in biological activity - ex: pharmacy - 2 enantiomers of a drug may not be equally effective (ex: crank vs. nasal inhaler) (mirrored versions of a molecule) | ![]() | 4 |
7269864316 | functional groups | may affect molecular function by being directly involved in chemical reactions - hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate, methyl | 5 | |
7269873639 | what do the functional groups hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate all have in common? | they are all hydrophilic, functional, and increase solubility of organic compounds in water | 6 | |
7269876936 | what is different between hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate functional groups and methyl? | methyl isn't reactive | 7 | |
7269877007 | hydroxyl group | -OH name: alochols (ex: ethanol) is polar because electrons spend more time near electronegative oxygen atom form hydrogen bonds with water helping dissolve organic compounds like sugars | ![]() | 8 |
7269884782 | carbonyl | name: ketones (in cytoskeleton), aldehydes (at end of C skeleton) ex: ketones - acetone ex: aldehydes - propanol can be structural isomers with different properties found in sugars. give rise to ketoses adn aldoses | ![]() | 9 |
7269892679 | carboxyl | name: carbolxyc acids ex: acetic acid acts as an acid - donates H+ becauses the covalent bond between O and H is so polar | ![]() | 10 |
7269900300 | amino | name: amines ex: glycine compounds with both amino and carboxyl group are amino acids acts as a base. picks up H+ from surrounding solution | ![]() | 11 |
7269903633 | sulfahydryl | name: thiols ex: cysteine- sulfur containing amino acid two groups react forming covalent bond. stabilizes protein structure (tertiary) cross linking in hair proteins maintains curls/straight hair | ![]() | 12 |
7269909165 | phosphate | name: organic phosphates ex: glycerol phosphate-phospholipids contributes negative charge when at end of molecules molecules with these groups have the potential to interact with water, releasing energy | ![]() | 13 |
7269914528 | methyl | name: methylated cmpds ex: methyl cytosine-component modified by methyl group affects expression of genes arrangement gives male and female sex hormones an affected shape and function | ![]() | 14 |
7269921656 | ATP | consists of organic molecule adenosine to which 3 phosphates are attached when reacts with water, third phosphate splits off releasing energy | 15 | |
7269925259 | macromolecules | carbs, proteins, nucleic acids, are huge | 16 | |
7269925287 | polymer | long macromolecule with many similiar building blocks with covalent bonds | ![]() | 17 |
7269927753 | monomers | repeating unit in polymers | ![]() | 18 |
7269927754 | enzymes | specializes macromolecules that speed up chemical reactions | ![]() | 19 |
7269930150 | dehydration synthesis | monomers connected in reaction in which 2 molecules are covalently bonded with loss of water molecule when bond forms, each monomer contributes either a -OH or -H to water molecules catalyzed by enzymes endergonic - needs energy | ![]() | 20 |
7269934581 | hydrolysis | - dissasembly of polymers - bond broken by additional addition of water - H+ attaching to one monomer and OH to another - exergonic - release of energy | ![]() | 21 |
7269936457 | carbohydrates | sugars and polymers of sugars | ![]() | 22 |
7269937568 | monosaccharieds | general formula CH2O - number of these units form a sugar vary | ![]() | 23 |
7269941105 | what kind of functional groups are in a sugar | a carbonyl and multiple hydroxyl groups | ![]() | 24 |
7270250771 | disaccharide | consists of 2 monosaccharides joined by glycosidic linkage | ![]() | 25 |
7270252913 | glycosidic linkage | covalent bond between 2 monosaccharides joined by dehydration reaction | ![]() | 26 |
7270262106 | polysaccharides | polymers with thousands of monosaccharides joined by glycosidic linkages | ![]() | 27 |
7270263991 | starch | -what plants store -polymer of glucose monomers, with plastids that have chloroplasts -synthesizing starch enables the plant to stockpile surplus glucose -is stored energy -can be withdrawn through hydrolysis, breaking down into glucose monomers -simplest form is amylose, then amylopectin (complex) -has alpha linkages ( repeating monomers in the same direction ) | ![]() | 28 |
7270275750 | glycogen | -what animals store -like amylopectin but more extensively branched - in muscle and liver cells -hydrolysis of glycogen releases glucose when the demand for sugar increases | ![]() | 29 |
7270284425 | cellulose | -tough outside wall that encloses plant cells - is unbranched - has beta glycosidic linkages -enzymes that digest starch by hydrolyzing alpha linkages can't do the same to cellulose because beta ones are a different shape. - some hydroxyls free to hydrogen bond with other hydroxyls to cellulose moleculse paralle to it -parallel cellulose held together by hydrogen bonds between hydroxyl groups attached to carbon - repeating units that are in opposite directions | 30 | |
7270303659 | beta linkages | monomers in alternating orientation (one upside down, the other right side up, etc) linkages in cellulose | ![]() | 31 |
7270307135 | alpha linkages | all monomers are in the same orientation linkages in starch | ![]() | 32 |
7279144204 | chitin | structural polysaccharide formed from glucose monomers - found in exoskeletons and fungi have nitrogen containing group | ![]() | 33 |
7279159298 | Lipids | fats, pospholipids, steroids hydrophobic do NOT form polymers | 34 | |
7279161018 | fats | fatty acids attached to the 3-carbon, alcohol, glycerol - are an excellent storage of molecules - twice the reserve of carbs | 35 | |
7279163193 | fatty acid | long, hydrocarbon chain with carboxyl group at one end - non polar hydrocarbons make them hydrophobic | ![]() | 36 |
7279169153 | triaglycerol | 3 fatty acids, each linked by an ester linkage- a bond between a hydroxyl and carboxyl | ![]() | 37 |
7279172118 | ester linkage | bond between hydroxyl and carboxyl | ![]() | 38 |
7279176600 | unsaturated fatty acids | fatty acids with double bonds in their carbon chain - is liquid at room temperature -cis double bond makes a kink - prevents unsaturated fatty acids from packing and solidifying together - plants and fish fat - oils - liquid at room temperature | ![]() | 39 |
7279183005 | saturated fatty acids | no double bonds animal fats solid at room temperature | ![]() | 40 |
7279184699 | trans fats | made in the process of hydrogenated vegetable oils unsaturated fats with trans double bond | ![]() | 41 |
7279196152 | phospholipids | glycerol linked to 2 fatty acids and a negatively charged phosphate group - phosphate head is hydrophilic - fatty acid tail is hydrophobic (ideal for membranes) | ![]() | 42 |
7279201204 | steroids | class of lipids distinguished by 4 connecting carbon rings with various attached groups - components of cell membranes (cholesterol) - signaling molecules that travel through the body (Horemones) | 43 | |
7279205389 | cholesterol | component in animal cell membranes - precursor for other steroids, including many hormones - help maintain fluidity in the cell membrane | ![]() | 44 |
7279210426 | catalysts | enzymes (proteins) that speed up reactions | ![]() | 45 |
7279210427 | polypeptide | polymer of amino acid | ![]() | 46 |
7279211659 | protein | functional molecule of one or more polypeptides, each folded in 3D shape | ![]() | 47 |
7279216743 | amino acids | - composed of alpha carbon bonded to a hydrogen atom, carboxyl group, amino group, variable side chain called R group - R group refers to unique physical and chemical properties - side chains may either be polar or charged and hydrophilic, or nonpolar and hydrophobic - amino and carboxyl usually ionized | ![]() | 48 |
7279222599 | examples of proteins | enzymes structural storage transport hormones receptor proteins motor proteins defensive proteins | 49 | |
7279227404 | peptide bond | bond linking carboxyl group of one amino acid with an amino acid of another - through dehydration reaction | 50 | |
7279230463 | N-terminus | amino end of polypeptide | 51 | |
7279231621 | C-terminus | carboxyl end of polypeptide | 52 | |
7279233944 | protein structure and function | amino acid sequence determines 3D shape - globular - sphere - fibrous - long fibers | 53 | |
7279238707 | what does the functionality of a protein depend on? | ability of the protein to recognize and bind to other molecules depends on molecular order also depends on physical and chemical enviornment | 54 | |
7279243049 | denaturation | protein loses native shape weak chemical bonds and interactions destroyed ex: when it moves from an aqueous to a nonpolar solvent ....... | 55 | |
7279247151 | chaperonins | protein molecules assist in folding of proteins keep new polypeptide segregated from bad influences in cytoplasmic environemnt from e. coli | 56 | |
7279250711 | xray crystallography | determines 3D structure of a protein | 57 | |
7279252442 | gene | amino acid sequence of a polypeptide programmed by a discrete unit of inheritance | ![]() | 58 |
7279256431 | nucleic acid | polymers made of monomers called nucleotides | ![]() | 59 |
7279257828 | deoxyribonucleic acid | enable organisms to reproduce their complex components through each generation | ![]() | 60 |
7279262593 | polynucleotides | nucleic acids make up polymers | ![]() | 61 |
7279264801 | nucleotide | made up of nitrogenous base, 5 carbon sugar (pentose), one or more phosphate groups | 62 | |
7279266392 | pyrimidine | one six membered ring of carbon and nitrogen atoms cytosine and thymine (remember: both contain a y in the name) | 63 | |
7279269306 | purines | larger, six membered ring fused to a five membered ring adenine and guanine | 64 | |
7279275832 | what are the different types of nitrogenous bases and who do they pair with | cytosine and guanine pair thymine and adenine pair | 65 | |
7279276984 | deoxyribose and ribose | - deoxyribose lacks an oxygen atom on the second carbon in the ring - second carbon is 2' - fifth carbon (sticks up from ring) is 5' | 66 | |
7279531842 | how to make a nucleotide | attach a phosphate group to the 5' carbon of the sugar which equals a nucleoside monophosphate = nucleotide | 67 | |
7279534050 | phosphodiester linkage | linkage between the phosphate group and sugars | ![]() | 68 |
7279537992 | double helix | 2 strands | ![]() | 69 |
7279537993 | antiparallel | 2 phosphate-sugar backbones rune in opposite 5' to 3' direction | ![]() | 70 |
7279541101 | complimentary | each side of DNA is predictable | ![]() | 71 |
7279542540 | primary structure | linked series of amino acids with a unique sequence - determined by inherited genetic info - LINEAR chain - dictates other structures, due to the back bone and variable side chains of the amino acids | ![]() | 72 |
7279545417 | secondary structure | regions stabilized by hydrogen bonds between atoms of polypeptide backbone - coils and folds of peptide chain due to the hydrogen bonds O atoms have partial (-) charge and H+ on Nitrogens have partial (+) charge, causing hydrogen bonds to form | ![]() | 73 |
7279553434 | what are the two types of secondary structures | alpha helix beta pleated sheet | ![]() | 74 |
7279554488 | alpha helix | form of secondary structure - delicate coil held by hydrogen bonding on every 4th amino acid | ![]() | 75 |
7279557929 | beta pleated sheet | 2+ strands of polypeptide chains side by side connected by hydrogen bonds between the 2 parallel peptide backbones | ![]() | 76 |
7279565661 | tertiary structure | 3D shape stabilized by interactions of the side chains (R groups) | ![]() | 77 |
7279569448 | hydrophobic interaction | interaction between amino acids with hydrophobic (nonpolar) side chains usually end up in clusters at core of protein. hydrophobic interaction caused by explosion of nonpolar substances by H20 molecules - once nonpolar amino acids are close to gether, van der waals hold them together - hydrogen bonds between polar side chains and ionic bonds help hold them together and stabilize the tertiary structure | ![]() | 78 |
7279576950 | disulfide bridges | covalent bonds from where 2 cytosine monomers, that have sulfhydryl groups on the side chain, are brought close together by folding of side chain | ![]() | 79 |
7279582075 | quaternary structure | overall protein structure that results from aggregation of polypeptide subunits - association of multiple polypeptides forming a functional protein | 80 | |
7279585029 | light microscope | visible light is passed through the specimen and then through glass lenses. bend light so specimin is magnitized (LIVE specimins) | 81 | |
7279587940 | magnification | ratio of objects size to true size of real image | 82 | |
7279588696 | resolution | measure of clairty of image | 83 | |
7279588697 | contrast | differences in parts of sample | 84 | |
7279589502 | electron microscope | focuses bam of electrons through specimines. study organelles better KILLS live specimines | 85 | |
7279591123 | scanning electron microscope | used for detail of topography - scans surface of sample | 86 | |
7279592913 | transmission microscope | study the internal structure of cells | 87 | |
7279594145 | cell fractionation | takes cells apart and separates major organelles and other subcellular structures from one another - centrifuge spins test tube. causes cell components to fall to bottom - allows researchers to prepare specific cell components in bulk and identify functions | ![]() | 88 |
7279603645 | cytosol | jelly fluid organelles are in | ![]() | 89 |
7279604591 | eukaryotic cells | DNA in nucleus that has a double membrane | ![]() | 90 |
7279605112 | prokaryotic | no nucleus - DNA in nucleoid | ![]() | 91 |
7279606159 | nucleoid | not membrane bound place where DNA is | ![]() | 92 |
7279606786 | cytoplasm | between nucleus and plasma membrane | ![]() | 93 |
7279607269 | plasma membrane | selective barrier allowing passage of oxygen, nutrients, waste - smaller objects have greater ratio of surface area to volume - necessary to exchange things across the barrier | ![]() | 94 |
7279609775 | nucleus | contains most of genes | ![]() | 95 |
7279610397 | nuclear envelope | encloses nucleus. double membrane | ![]() | 96 |
7279610398 | nuclear lamina | netlike array of protein filaments that maintains the shape of nucleus by supporting nuclear envelope - nuclear lamina and filaments help organize genetic material | ![]() | 97 |
7279619711 | chromosomes | structures carrying genetic info | ![]() | 98 |
7279621574 | chromatin | complex of DNA and proteins in chromosome | ![]() | 99 |
7279622884 | nucleolus | -nondividing structure in nucleus -synthesis of rRNA -combines rRNA with protein to assemble ribosomal subunits, then passes through nuclear pores | ![]() | 100 |
7279626562 | ribosomes | made of protein and ribosomal RNA - free - in cytosol - bound - attached to ER- make proteins in membranes, packed in organelles, or exported out of cell | ![]() | 101 |
7279629243 | endomembrane system | nuclear envelope, endoplasmic reticulum, golgi, lysosomes, vesicles, vacuoles, plasma membrane membranes related through contact or vesicles | ![]() | 102 |
7279630710 | vesicles | membrane bound sacs that transfer membrane segments | ![]() | 103 |
7279635942 | ER | - membranous system continuous with nuclear envelope and enclosed in a network of interconnected tubules or compartments called cisternae | ![]() | 104 |
7279636898 | Rough ER | has ribosomes attached proteins meant for secretion made by ribosomes then threaded through lumen of RER. most proteins are glycoproteins | ![]() | 105 |
7279640812 | glycoproteins | proteins covalently bonded to small carbohydrates | ![]() | 106 |
7279637501 | Smoother ER | doesn't have ribosomes attached enzymes involved in phospholipid and steroid synthesis, carbohydrate metabolism, detox of drugs and poisons, storage release of Ca ions during muscle contraction - alcohol makes liver increase production of smooth ER, leading to increased tolerance | ![]() | 107 |
7279646582 | transport vesicles | what proteins are transported in from RER | ![]() | 108 |
7279653200 | Golgi | stack of flattened sacs - golgi products are processed and tagged as cisternae - products of ER are modified and stored and transported to other places | ![]() | 109 |
7279658786 | what are the two faces of the golgi body | CIS and TRANS | 110 | |
7279659459 | what is the CIS face of the Golgi | CIS - near ER - side of ER - entrance of stuff | 111 | |
7279660104 | what is the TRANS face of the golgi | TRANS - gives rise to vesicles pinching off and traveling to other sites carrying golgi products - of plant manufactures polysaccharides | 112 | |
7279662518 | lysosomes | membrane enclosed sacs containing hydrolytic enzymes that digest macromoleucules - can provide acidic pH for these enzymes - recycles cells own macromolecules by fusing with damaged organelles | ![]() | 113 |
7279665425 | autophagy | when lysosomes fuse with damaged organelles to recycle them | ![]() | 114 |
7279667637 | vacuoles | large vesicles | ![]() | 115 |
7279669286 | phagocytosis | when protists engulf particles how lysosomes can digest food vacuoles | ![]() | 116 |
7279667638 | food vacuoles | as a result of phagocytosis stores food | 117 | |
7279671543 | contractile vacuoles | pump excess water out of fress water protists | 118 | |
7279672259 | what can vacuoles in plant cells do | can store organic and inorganic ions, contain dangerous metabolic byproducts, protect plant from predators | 119 | |
7279673734 | central vacuole | found in mature plant cells contain solution called cell sap | ![]() | 120 |
7279674365 | mitochondria | where cellular respiration happens to make ATP | ![]() | 121 |
7279678772 | cisternae | folds of membrane of mitochondria create a large surface area enclose mitochondria matrix | ![]() | 122 |
7279675545 | endosymbiont theory | mitochondria was prokaryote - mitochondria has 2 membranes, phospholipid bilayer with special proteins, own DNA, ribosomes | ![]() | 123 |
7279677673 | chloroplasts | where photosynthesis happens makes sugars from CO2, H2) and solar energy have 2 membranes | ![]() | 124 |
7279681158 | thylakoids | intermembrane system of connected sacs in chloroplasts | ![]() | 125 |
7279681807 | grana | stacks of thylakoids | ![]() | 126 |
7279681808 | stroma | fluid fillid around the thylakoids contain chloroplast DNA, ribosomes, enzymes | ![]() | 127 |
7279683194 | plastids | plant organelle (chloroplasts) include amyloplasts which stores starch, chromoplasts which contain pigments | ![]() | 128 |
7279684383 | amyloplasts | type of plastid that stores starch | ![]() | 129 |
7279684795 | peroxisomes | specialized metabolic compartment bound by a membrane contain enzymes that remove hydrogen atoms from substrates and transfer them to oxygen to make hydrogen peroxide (H202) | ![]() | 130 |
7279687787 | function of peroxisomes | - break down fatty acids for energy, detox alochol and poisons - has enzymes that converts hydrogen peroxide to water - glyoxysomes | 131 | |
7279690591 | glyoxysomes | Specialized peroxisomes found in the fat storing tissues of plant seeds - convert fatty acids to sugars | ![]() | 132 |
7279701034 | cytoskeleton | network of protein fibers give mechanical support and function in cell mobility interacts with motor proteins to produce cellular movements | 133 | |
7279722788 | microtubules | - hollow rods constructed of colums of globular proteins called tublins. thickest . ex: separate chromosomes during cell division - are tracks taht roganelles move along with aid of motor proteins - grow out of centrosome | ![]() | 134 |
7279765721 | centrosome | region near nucleus called microtuble organizing center | 135 | |
7279766159 | centrioles | part of centrosome pair of centrolies, each made of 9 sets of triplet microtubules in a ring, is associated with centrosome and replicated before cell divison | 136 | |
7279770794 | cilia and flagella | locomoter extensions both composed of 2 single microtubules surrounded by a ring of 9 doublets of microtubules enclosed in extension of plasma membrane | ![]() | 137 |
7279772029 | basal body | with "9+0+ pattern of microtubule triplits, anchors a cilium or flagellum in cell. | 138 | |
7279773225 | dyneins | large motor proteins composed of several polypeptides -responsable for bending movement of organism - atp provides energy to allow dynein proteins to change shape to preform complex movements | ![]() | 139 |
7279776644 | microfilament | smallest solid rods build from actin is a twisted chain of actin subunits form a structural network when proteins bind to side of actin filament structural purpose is to bear tension (pull force) and support the shape of the cell | ![]() | 140 |
7279776645 | actin | globular protein. units of microfilament | ![]() | 141 |
7279779681 | cortex | outer cytoplasmic layer of cell microfilament structure gives the cortex its gel consistency - microfilaments increase surface area of intestinal cells - microfilaments on length of muscle cell with myosin | 142 | |
7279782789 | myosin | thicker filaments made of a protein acts as a motor protein- walks along actin filaments contraction of a muscle cell is bc of actin and myosin filaments sliding past another, shortening of cell | ![]() | 143 |
7279785095 | cytoplasmic streaming | involves both actin myosin interactions and sol-gel conversions - circular flow of cytoplasm in cells | ![]() | 144 |
7279786154 | intermediate filaments | smaller than microtubules, bigger than microfillaments maintain cell shape nucleus security held by web of intermediate fillaments nuclear lamina made of intermediate filaments -permanent network of cell | ![]() | 145 |
7279788370 | cell wall | composed of microfibrils of cellulose embedded in a matrix of polysaccharides and protein | ![]() | 146 |
7279789505 | microfibrils | made of polysaccharide cellulose synthesized by cellulose synthase | ![]() | 147 |
7279789504 | primary cell wall | young plant thin and flexible microtubules in cell cortex guide path of cellulose synthase, determining pattern of cellulose fibril deposition and thus direction of cell expansion | ![]() | 148 |
7279792169 | middle lamella | between primary walls of adjacent cells - thin layer of polysaccharides (PECTIN) | ![]() | 149 |
7279793134 | secondary wall | between plasma membran and primary cell wall | ![]() | 150 |
7279793889 | extracellular matrix | made of glycoproteins and other carbohydrae containing molecules | ![]() | 151 |
7279794344 | glycoproteins | are proteins covalently bonded with carbs, usually in sort chain fo sugars | ![]() | 152 |
7279795452 | collagen | forms strong fibers embedded in a network of proteoglycan complexes (outside of cell) | ![]() | 153 |
7279796890 | proteoglycans | consist of small core protein with many carbohydrate chains all attached to long polysaccharides | ![]() | 154 |
7279797498 | fibronectins | how cells attach to ECM | ![]() | 155 |
7279797513 | integrins | span plasma membrane. what fibronectins bind to bind to microfilaments bind to micro filaments via other proteins of cytoskeleton | ![]() | 156 |
7279807511 | plasmodesmata | channels in plant cell walls which plasma membranes connect linking plant cells into a living continuoum | ![]() | 157 |
7279808926 | tight junction | proteins hold adjacent membranes tightly together creating impermeable seal across layer of epithelial cells - prevent leakage | ![]() | 158 |
7279811104 | desmosomes | reinforced by intermediate filaments. rivet cells into strong sheets (in muscle) | ![]() | 159 |
7279813304 | gap junction | cytoplasmic connections allow for exchange of small molecules and ions between cells to protein lined pores | ![]() | 160 |
7279815897 | fluid mosaic model | biological membranes consist of various proteins that are attached to or embedded in bylayer of phospholipids | 161 | |
7279817699 | amphipathic | both hydrophilic and phdrophobic | 162 | |
7279819242 | parts of plasma membrane | - membranes held together by weak hydrophobic interactions that allow the lipid and some of the proteins to drift laterally - soe membrane proteins held by cytoskeleton or ECM - others directed in movements - phospholipids with unsaturated carbon tails maintain membrane fluidity at a lower temp | 163 | |
7279822468 | cholesterol | restricts movement of phospholipids reducing fluidity at warmer temps and enhancing fluidity at lower temps | 164 | |
7279823709 | integral proteins | extended though membrane with 2 hydrophilic ends and a hydrophobic midsection made of one or more alpha helical structures of nonpolar amino acids | 165 | |
7279825228 | peripheral proteins | attached to surface of membrane - attachments of membrane proteins to cytoskeleton and fibers of ecm provide support for membrane | 166 | |
7279826800 | glycolipids | cacarbs covalently bonded to lipids | 167 | |
7279828129 | what do glycolipids and glycoproteins have to do with the plasma membrane | the diversity and location of these molecules enable membrane carbs to funciton as markers that distinguish one cell to another | 168 | |
7279828965 | channel proteins | have hydrophilic channel to allow passage of polar molecules | 169 | |
7279829518 | transport proteins | help move ions and polar molecules across membrane | 170 | |
7279829820 | aquaporins | allows passage of water through membranes | 171 | |
7279829821 | diffusion | movement of substance down conentration gradient due to random thermal motion | 172 | |
7279830743 | passive transport | no energy expenditure | 173 | |
7279830744 | osmosis | diffusion of free water across permeable membrane. diffuses down concentration gradient | 174 | |
7279831536 | tonicity | clustering of water around solute adn free water particles tendency of a surrounding solution to gain or lose water | 175 | |
7279832515 | isotonic | neigher gain or lose water | 176 | |
7279833194 | hypertonic | more non-penetrating solutes - water will flow out of cell when it is in a hypertonic environment, causing it to shrivel | ![]() | 177 |
7279835490 | hypotonic | less solutes outside of cell than inside, cause water to go into cell and burst | 178 | |
7279836533 | turgid | firm, healthy state for plant cells turgor pressure water moving in cell causes cell to swell against cell wall | ![]() | 179 |
7279837302 | flaccid | plant clels in isotonic surrounding (limp) | ![]() | 180 |
7279837761 | plasmolysis | plasma membrane pulls away from cell wall as water exists and cell shrivels, when in hypertonic solution | ![]() | 181 |
7279840569 | facilitated diffusion | diffusion of polar molecules with the aid of transport proteins | ![]() | 182 |
7279841292 | ion channel and gated channels | open and close in response to electrical stimuli | ![]() | 183 |
7279841937 | active transport | requires energy to transport ATP phosphate group may be transferred to carrier protein, making it change shape and translocate from bound solute to membrane | ![]() | 184 |
7279843235 | sodium potassium ion pump | exchanges Na and K across animal cell membranes, creating a high concentration of K ions and a low concentration of sodium ions in cell | ![]() | 185 |
7279844527 | membrane potential | voltage across a membrane - favors transport of cations into cell because inside is negative and outside is positive | ![]() | 186 |
7279846291 | electrochemical gradient | combination of forces acting on ion - chemical - conecntration gradient - electrical - effect of membrane potential | ![]() | 187 |
7279847272 | proton pump | transports H out of cell and generates voltage across membrane in plants, fungi and bacteria | ![]() | 188 |
7279849724 | cotransport | mechanism through which the active transport of a solute is indirectly driven by an ATP powered pump that transports another substance down its gradient - as the actively transported substance diffuses back down its concentration gradient through cotransporter, the solute is carried against concentration gradient across membrane | ![]() | 189 |
7279852445 | exocytosis | cell secretes large molecules by the fusion of vesicles with the plasma membrane | ![]() | 190 |
7279852999 | phagocytosis | form of endocytosis -pseudopodia wrap around a food particle adn engulf it, creating a vacuole - fuses with lysosome | ![]() | 191 |
7279854178 | pinocytosis | droplets of extracelluar fluid taken into the cell in small vesicles | ![]() | 192 |
7279854602 | receptor mediated endocytosis | enables a cell to aquire specific substances from extracellular fluid | ![]() | 193 |
7279855261 | ligands | molecules that bind to receptor cites - attach receptor proteins (usually coated in clustered pits on cell surface) and are carried into cell when vesicle forms | ![]() | 194 |
AP Biology Chapters 4-7 Flashcards
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