Terms : Hide Images
| 6219746574 | alpha helix | secondary structure A spiral shape constituting one form of the secondary structure of proteins, arising from a specific hydrogen-bonding structure. Proline and glycine | 0 | |
| 6219747731 | Beta-pleated sheets | Secondary structure backbone hydrogen bonding between adjacent parallel or anti-parallel polypeptides assume a pleated shape (amino residues point in alternation above and below) | 1 | |
| 6219747732 | 1/2 Vmax | Km is the concentration of 1/2 Vmax competitive inhibition increases Km Uncompetitve inhibition decreases Km, 1/2 vmax, Vmax Mixed inhibition decreases/increases Km, decreases 1/2 vmax, decreases Vmax | 2 | |
| 6219748533 | Active site | The part of an enzyme or antibody where the chemical reaction occurs. Substrate binds to the enzyme at this particular location. | 3 | |
| 6219748534 | Adenine | it is a purine it pairs with Thymine | 4 | |
| 6322813400 | Urea denatures | H Bonds | 5 | |
| 6322814692 | Salt or change in pH effects | Electrostatic bonds in proteins | 6 | |
| 6322819725 | Beta Mercaptoethanol | Disulfide Bonds | 7 | |
| 6322821014 | Organic solvents | Hydrophobic Forces | 8 | |
| 6322822946 | Heat denatures... | all forces(h-bonds, disulfide, electrostatic, | 9 | |
| 6219749585 | Adipocytes | Fat cells specialized fat cells whose cytoplasm contains nothing but triglycerides | 10 | |
| 6219749586 | allosteric activators | assist the enzyme by building the enzyme on a site other than the active site to boost the activivty. bind tightly to the high affinity R state of the enzyme than the T state. Activators increase the amount of enzyme in the active state, thereby facilitating substrate binding in their own and other subunits. | 11 | |
| 6219753596 | Allosteric inhibitors | modify the active site of an enzyme so that substrate binding is reduced/prevented. bind more tightly to the T state, which means either substrate concentration or activator concentration must be increased to overcome the effect of the inhibitor | 12 | |
| 6219753597 | Allosteric interactions | when a molecule binds and a conformational change occurs and the primary binding site will be changed to either bind the substrate more tightly or not bind it tightly at all. | 13 | |
| 6219754777 | allosteric regulations | When a protein's function at one site is affected by the binding of a regulatory molecule to a separate site. | 14 | |
| 6219754778 | Amide | RCONH2 | 15 | |
| 6219754779 | Amino Acids | Building blocks of proteins Monomer of Proteins | 16 | |
| 6219755575 | Amphipathic and example | A molecule that has both a hydrophilic region and a hydrophobic region. phospholipids | 17 | |
| 6219755576 | Antiparallel | The opposite arrangement of the sugar-phosphate backbones in a DNA double helix. 5-3 and 3-5 | 18 | |
| 6219757052 | ATP(adenosine triphosphate | High energy nucleotide that runs that life of the cell. made by glycolysis and Krebs cycle | 19 | |
| 6219757053 | Base-pairing | A - T 2 H bonds G- C 3 H bonds holds dan together in a double helix through H bonds principle that bonds in DNA can form only between adenine and thymine and between guanine and cytosine | 20 | |
| 6219757896 | Base-pairs bp | A - T 2 H bonds G- C 3 H bonds | 21 | |
| 6219757897 | carbohydrates | "Compound containing carbon, hydrogen, and oxygen in the approximate ratio of C:2H:O (e.g., sugars, starches, and cellulose)" Main source of energy | 22 | |
| 6219758936 | Catalyst | (chemistry) a substance that initiates or accelerates a chemical reaction without itself being affected The lower the activation energy of a reaction and thereby increasing the rate | 23 | |
| 6219758937 | Cellulose | ß-1,4 linkage Carbohydrate component of plant cell walls. | 24 | |
| 6219822132 | Why can we not digest cellulose | ß-1,4 linkage and we don't have the enzymes to break this down. | 25 | |
| 6219759965 | Coenzymes | Organic Cofactors An organic molecule that is a necessary participant in some enzymatic reactions; helps catalysis by donating or accepting electrons or functional groups; e.g., a vitamin, ATP, NAD+. | 26 | |
| 6371715577 | two subgroups of coenzymes | cosubstrates and prosthetic groups | 27 | |
| 6219759966 | Cofactors | Any nonprotein molecule or ion that is required for the proper functioning of an enzyme. Cofactors can be permanently bound to the active site or may bind loosely with the substrate during catalysis | 28 | |
| 6219761224 | Difference between cofactor and coenzyme | Coenzyme has to be organic, normally an enzyme, a coenzyme can be a cofactor | 29 | |
| 6219762607 | competitive inhibitors. | A substance that reduces the activity of an enzyme by entering the active site in place of the substrate whose structure it mimics. It increases the Km has no effect on Vmax Inhibitor that competes for binding at the enzyme active site | 30 | |
| 6219763181 | Complementary strands | relation between two nucleotide strands of DNA in which each purine on one strand pairs with a specific pyrimidine on the opposite strand - A and T; C and G | 31 | |
| 6219764439 | conformational change | an alteration of the structure of the protein that impacts that protein's function | 32 | |
| 6219765560 | Cysteine why is it important | its an amino acid that can make disulfide bonds | 33 | |
| 6219765561 | Cystine | cysteine cystein dimer with a dissulfide bridge bond | 34 | |
| 6219767000 | Difference between Cystine and Cysteine | cysteine cystein dimer with a dissulfide bridge bond | 35 | |
| 6219768027 | Cytosine | C pyrimidine that binds with G 3 h bonds | 36 | |
| 6219768719 | Dehydration | the formation of bonds the formation of a peptide bond product is water two molecules come together to form a bond. | 37 | |
| 6219770579 | Dehydration reactions do what to bonds? | Formation of a bond | 38 | |
| 6219770580 | Denatured | loss of native fold of proteins An uncoiled, or unraveled protein, the protein has lost its shape due to high temperatures or strong chemicals, its weak bonds have broken and the protein cannot perform its job, since it no longer "fits" with other molecules | 39 | |
| 6322961070 | there are two types of proteins what are they? | Globular and structural | 40 | |
| 6219772763 | What process denature native protein folds | Heat, Urea, beta mercaptoethanol, SDS, Salt and Ph | 41 | |
| 6219786001 | DNA (deoxyribonucleic acid) | A molecule that carries the genetic code for all living organisms. | 42 | |
| 6219786870 | Differences between DNA and RNA | 1. RNA has ribose suga 1. DNA is the "Master plan" and RNA is the "inexpensive blueprints DNA-Double helix RNA-Single heli RNA is single stranded, DNA is double stranded |  | 43 |
| 6219786871 | Double Helix | The form of native DNA, referring to its two adjacent polynucleotide strands wound into a spiral shape. |  | 44 |
| 6219788298 | WHy DNA goes into a double helix | H bonds Negative back bone the major and minor grooves have 10 base pairs per spiral | 45 | |
| 6219806957 | Entropy Definition | measure of disorder is a measure or randomness or disorder, symbol S | 46 | |
| 6219809376 | Entropy and how that it is involved in Enzymes catalytic activity | Enzymes lower activation energy and the interactions between enzyme active site and substrates are more favorable for entropy | 47 | |
| 6219810491 | Enzyme Specificity | Enzymes will only catalyze a single reaction or class of reactions with theses substrates. There are six categories. enzymes are designed to work only on a specific substrate or group of closely related substrates | 48 | |
| 6371770105 | a tight fit represents what type of Km? | a Lower Km | 49 | |
| 6371774818 | a lower Km means what about the fit in the enzyme | tight fit | 50 | |
| 6219810492 | Enzyme-substrate complex | A temporary complex formed when an enzyme binds to its substrate molecule(s). formed by the temporary binding of enzyme and reactants enables the collisions to be more effective and LOWERS THE ACTIVATION ENERGY OF THE REACTION | 51 | |
| 6219812260 | Enzymes | Catalysts for chemical reactions in living things | 52 | |
| 6371797754 | 6 Types of Enzymes | 1. hydrolases 2. isomerases 3. ligases or polymerases 4. lyases 5. oxidoreductases 6. transferases | 53 | |
| 6219812261 | Enzymes function | controls rates of metabolic rxns by lowering activation energy | 54 | |
| 6219814844 | E + S => ES => E + P | represents what is happening with the enzyme and substrate and products. the second reaction is fast and doesn't really have an equilibrium. | 55 | |
| 6371820757 | How am I supposed to be able to tell the difference between the different types of enzyme inhibition? | where does it bind? to the active site or an allosteric site or Enzyme or the ES complex | 56 | |
| 6219817093 | fats-soluble vitamins |  | 57 | |
| 6372157809 | water versus fats-soluble vitamins |  | 58 | |
| 6219817094 | Fats | Lipids non polar used for enery |  | 59 |
| 6371846115 | 3 roles of Lipids in cells | 1. Energy storage (fatty acids) 2. Cellular organization and structures(cell membrane) 3. Provision of precursor molecules for vitamins and hormones. | 60 | |
| 6219817095 | Fatty acids | they are fuel for the body and are components of the cell membrane. | | 61 |
| 6219818621 | Three functions of Lipids in the Body | 1. Energy storage (fatty acids) 2. Cellular organization and structures(cell membrane) 3. Provision of precursor molecules for vitamins and hormones. | 62 | |
| 6219819866 | Feedback inhibitions | Negative feedback stops the output. as product is formed from a process those same products inhibit the formation of more products. many forms of this but prevalent in metabolism. the mechanism in which the end product of a metabolic pathway inhibits an earlier step in the pathway is most precisely described as | 63 | |
| 6219819867 | Glucose pyranose |  | 64 | |
| 6371930149 | fisher projection of glucose |  | 65 | |
| 6371933174 | Glucose is always in what form in nature? | D-glucose | 66 | |
| 6371927374 | Glucose | main source of energy. Body uses it in Glycolysis and for metabolism and everything. also to store energy. | 67 | |
| 6371921673 | Glucose linear |  | 68 | |
| 6219832517 | Glycerol | A three-carbon alcohol to which fatty acids are covalently bonded to make fats and oils. |  | 69 |
| 6219832518 | Glycogen | An extensively branched glucose storage polysaccharide found in the liver and muscle of animals; the animal equivalent of starch. |  | 70 |
| 6371957560 | Glycogen connections | alpha-1,4 linkages(linear) and alpha-1,6 linkages(branches) | 71 | |
| 6371972526 | alpha-1,6 linkages serve what purpose in glycogen | they make branches and aren't able to broken down. | 72 | |
| 6371966421 | Glycogen linkages that can be broken down? | alpha-1,4 linkages | 73 | |
| 6219833184 | Glycogon | Hormone that changes glucose into glycogen moves glucose from cell to blood hormone of pancreas; secreted by alpha cells of islets; promotes hydrolysis of glycogen in the liver and fat in adipose tissue | 74 | |
| 6219833185 | Guanine | Purine A component of nucleic acids that carries hereditary information in DNA and RNA in cells. Chemically, it is a purine base. |  | 75 |
| 6371984360 | C-G base pair | 3 bonds |  | 76 |
| 6219833186 | Hexoses | 6 carbon carbohydrates examples are fructose and glucose |  | 77 |
| 6219835216 | Hydrogen Bonding | the intermolecular force in which a hydrogen atom that is bonded to a highly electronegative atom is attracted to an unshared pair of electrons of an electronegative atom in a nearby molecule important in DNA and Protein structure and everything in BIOlogy |  | 78 |
| 6219837363 | How is h bonding important in DNA, water and what not | it gives needed stability and drives reactions and makes surface tension and does everything | 79 | |
| 6219838119 | Hydrolases | catalyze cleavage with the addition of water Chymotrypsin is a protease that cleaves peptide bonds. It is characterized as which of the following classes of enzymes? |  | 80 |
| 6219838120 | Hydrolysis | Breaking down complex molecules by the chemical addition of water Breaking Bonds |  | 81 |
| 6219839794 | What does Hydrolysis do to bonds? | breaks them with a water molecule. | 82 | |
| 6219840485 | Hydrophilic | Having an affinity for water Water loving Polar | 83 | |
| 6219840486 | Hydrophobic | Having an aversion to water; tending to coalesce and form droplets in water. non-polar important in protein structure | 84 | |
| 6219841502 | Hydrophobic bonding how it happens and why? | This really happens because water has a higher level of entropy when the hydrophobic things are sequestered together so the desire for entropy squishes the hydrophobic molecules together. | 85 | |
| 6219842631 | Why is hydrophobic bonding favorable in an aqueous solution | Entropy of water is higher when hydrophobic molecules are grouped together. | 86 | |
| 6219845276 | Induced Fit model | Change in the shape of an enzyme's active site that enhances the fit between the active site and its substrate(s) |  | 87 |
| 6372098874 | Glycoproteins | A protein with one or more covalently attached carbohydrates. Membrane carbohydrates that are covalently bonded to proteins. |  | 88 |
| 6372098875 | proteoglycans | Long, linear, unbranched polysaccharides attached to protein macromolecules constucted of a protein core which glycosaminoglycans are attached |  | 89 |
| 6372101964 | cytochromes | have nonprotein parts like iron (donate/accept electrons, for redox!) are proteins which require a prosthetic heme group in order to function. An iron-containing protein that is a component of electron transport chains in the mitochondria and chloroplasts of eukaryotic cells and the plasma membranes of prokaryotic cells |  | 90 |
| 6219846081 | irreversible inhibitors | forms a covalent bond with an amino acid side group within the active site, which prevents that substrate from entering the active site, or prevents catalytic activity |  | 91 |
| 6219848151 | what does competitive inhibitors due to a lineweaver plot | 92 | ||
| 6219849810 | what does noncompetitive inhibitors due to a lineweaver plot | 93 | ||
| 6219849811 | what does uncompetitive inhibitors due to a lineweaver plot | 94 | ||
| 6219932480 | what does mixed inhibitors due to a lineweaver plot | 95 | ||
| 6219935866 | isomerases | catalyze the rearrangement of bonds within a molecule |  | 96 |
| 6219936860 | 6 types of enzymes | 1. hydrolases 2. isomerases 3. ligases or polymerases 4. lyases 5. oxidoreductases 6. transferases | 97 | |
| 6219938471 | Km | What substrate concentration is required to produce 1/2 Vmax? |  | 98 |
| 6219938472 | what does Km mean | - High KM means a low affinity low Km means a high affinity reflects how well substrate binds to the enzyme | 99 | |
| 6219939099 | Ligases | catalyze condensation reactions coupled with the hydrolysis of high energy molecules catalyze addition or synthesis reactions, generally between large similar molecules, and often require ATP | 100 | |
| 6219939100 | Lipids | Energy-rich organic compounds, such as fats, oils, and waxes, that are made of carbon, hydrogen, and oxygen. | | 101 |
| 6219939101 | Lock and KEy model | Enzymes are specific. The only wok on the substrate that they "fit." Just like a lock has a specific key to open it. The model that states that the shape of an enzyme and that of the reactants is what allows the enzyme to bind specifically and easily to the reactant One type of enzyme fits one type of molecule. Change its shape and the enzyme will no longer work |  | 102 |
| 6219940203 | Compare and contrast the Lock and key model and the induced model | The lock and Key model fits some enzyme models but the more accepted model is the induced model and it says the shapes of both the enzyme and the substrate are altered upon binding. | 103 | |
| 6219940204 | Lyases | catalyze cleavage without the addition of water and without the transfer of electrons catalyze reactions in which functional groups are added to double bonds or, conversely double bonds are formed via the removal of functional groups | 104 | |
| 6219941283 | Michaelis constant | it is the Km or 1/2 Vmax. | 105 | |
| 6219941284 | Minerals | Nutrients that are needed by the body in small amounts and are not made by living things Elements found in food that are used by the body | 106 | |
| 6219941728 | Mixed inhibitors | 107 | ||
| 6219942479 | Monosaccharides | 108 | ||
| 6219942480 | negative cooperation | 109 | ||
| 6219945423 | Difference between negative and positive cooperations | 110 | ||
| 6219945424 | Negative Feedback | 111 | ||
| 6219946597 | Noncompetitive inhibitors | 112 | ||
| 6219946598 | Nucleic Acids | 113 | ||
| 6219947207 | Nucleosides | 114 | ||
| 6219947208 | Nucleotides | 115 | ||
| 6219948461 | A and T how many H Bonds | 116 | ||
| 6219949219 | G and C how many H bonds | 117 | ||
| 6219950360 | Oxidoreductases | catalyze oxidation-reduction reactions that involve the transfer of electrons |  | 118 |
| 6219950361 | Phosphotids | 119 | ||
| 6219951913 | Phosphodiester bonds | A bond formed between adjacent nucleotides which consists of a phosphate group that links the sugars of two nucleotides |  | 120 |
| 6219953151 | phospholipids | A molecule that is a constituent of the inner bilayer of biological membranes, having a polar, hydrophilic head and a nonpolar, hydrophobic tail. |  | 121 |
| 6219953152 | Polypeptides | 122 | ||
| 6219954539 | Polysaccharides | 123 | ||
| 6219955192 | Positive Cooperation | 124 | ||
| 6219955894 | Positive feedback | A type of regulation that responds to a change in conditions by initiating responses that will amplify the change. Takes organism away from a steady state. A physiological control mechanism in which a change in some variable triggers mechanisms that amplify the change. |  | 125 |
| 6219956668 | Primary Protein Structure | sequence of amino acids The first level of protein structure; the specific sequence of amino acids making up a polypeptide chain. |  | 126 |
| 6376095486 | protein structure groups picture |  | 127 | |
| 6219957400 | Proline and secondary and tertiary structures | it adds kicks to the beta pleated sheets and alpha helices so you won't see it ther kinks the chain, thus never found in alpha helix Introduces kinks into the secondary structure-- should not be found in the middle of alpha helices or beta sheets but are good for the turns of beta sheets and the start of alpha helices. | 128 | |
| 6219957401 | Prostaglandins | Eicosanoid A group of bioactive, hormone-like chemicals derived from fatty acids that have a wide variety of biological effects including roles in inflammation, platelet aggregation, vascular smooth muscle dilation and constriction, cell growth, protection of from acid in the stomach, and many more. | 129 | |
| 6219957812 | Purines | Adenine and Guanine |  | 130 |
| 6219957813 | Pyrimindines | Thymine and cytosine |  | 131 |
| 6219959108 | the difference between Purines and Pyrimindines | Two rings instead of one on purines | 132 | |
| 6219959109 | Quaternary Structures | 133 | ||
| 6219959848 | RNA | 134 | ||
| 6219959849 | Saturated Fatty acids | 135 | ||
| 6219960423 | Saturation Kinetics | 136 | ||
| 6219961045 | Secondary structure | 137 | ||
| 6219961046 | Side chain | 138 | ||
| 6219961047 | R groups | 139 | ||
| 6219963876 | single stranded RNA | 140 | ||
| 6219963877 | Solvation layer | 141 | ||
| 6219964759 | Sphingolipids | 142 | ||
| 6219964760 | Starch | 143 | ||
| 6219965331 | Structure of starch | 144 | ||
| 6219965332 | Steriods | 145 | ||
| 6219965333 | Substrates | The reactants that are affected by enzymes in enzyme-catalyzed reactions. reactants of enzyme-catalyzed reactions |  | 146 |
| 6219966162 | Substrate concentration and its effects | 147 | ||
| 6219966163 | Sugar-phosphate backbone | 148 | ||
| 6219967829 | tertiary Structure | 149 | ||
| 6219967830 | Thymine | 150 | ||
| 6219968680 | Transferase | 151 | ||
| 6219969481 | triacyclglycerols | 152 | ||
| 6219969482 | Triglycerides | 153 | ||
| 6219970226 | uncompetitive inhibitors | They bind at a site other than the active site causing a conformational change in the protein | 154 | |
| 6219970632 | Unsaturated Fatty acids | 155 | ||
| 6219970633 | Uracil | binds with Adenosine. |  | 156 |
| 6219970634 | vitamins | Compounds found in food that help regulate many body processes | 157 | |
| 6219970643 | Water | H2O |  | 158 |
| 6219971719 | Water-soluble vitamins | They are coenzymes b and C vitamins | 159 | |
| 6219972664 | Watson-crick model | the 3D model of DNA DNA double helix consists of 2 nucleotide strands held together by hydrogen bonds between bases | 160 | |
| 6219972665 | waxes | A type of lipid molecule consisting of one fatty acid linked to an alcohol; functions as a waterproof coating on many biological surfaces such as apples and other fruits. | 161 | |
| 6219974057 | Vmax | The maximum rate of an enzymatic reaction, attained immediately after the addition of substrate at a concentration sufficient to fully occupy the active sites of all enzyme molecules present. | | 162 |
| 6219974058 | zymogen | An inactive precursor of an enzyme, activated by various methods (acid hydrolysis, cleavage by another enzyme, etc.) A protein that is an inactive precursor of an enzyme | 163 | |
| 6219975264 | why are zymogen's important | it allows for protein activation when you needed and also allows for activation of the protein in certain circumstances so when the protein is needed it is activated. | 164 |
