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Ap Bio Mod 13-14
| Question | Answer |
|---|---|
| Kinetic energy | the energy of movement -three types: Light energy, thermal energy, electric energy |
| potential energy | -stored energy (stored in bonds in chemical reactions) -energy that depends on the structure of object or postion |
| Chemical energy | -a type of potential energy which is held in chemical bonds |
| Relationship Between Chemical energy and chemical bond strength | - the stronger the bond, the less the chemical energy ( less chemical energy is needed to hold them together) - the weaker the bond, the more chemical energy (more chemical energy is needed to hold them together) |
| Metabolic pathway | a linked sequence of chemical reactions which consists of several different chemical reactions, and each chemical reaction constitutes a step in the pathway. |
| effect of high free energy on system | -decreases stability -increases work capacity - tries to move system close to equilibrium |
| effect of low free energy on system | -increases stability -decreases work capacity - makes system close to equilibrium |
| Metabolic pathways | -a series of chemical reactions that occur in the cell where molecules are built up or broken down -the product of one chemical reaction is used as fuel for the next |
| Cofactor | molecules that bind to enzymes and are necessary for their functioning - specific example is coenzyme |
| Heat | -the most random form of energy -increases entropy |
| activation energy | -the energy that must be absorbed by molecules in order to reach transition state -enzymes lower activation energy needed, allow reactions to start at a faster rate |
| feedback inhibition | -when the product of one reaction is used to stop enzymes from making more products -the product acts as a inhibitor by do so |
| What happens as you continue to increase substrate concentration | - the speed of enzyme reaction increases until enzyme become complete filled with substrates (saturated) upon which the rate of reaction will stop increasing and stay constant -you reduce the competition between competitive inhibitors and substrates and |
| What are optimal conditions? (optimal ph and optimal temperature) | -the conditions in a enzymes every in which it functions the best and is most active |
| Competitive inhibitors | -an inhibitor that resembles the normal substrate and binds to the enzyme at the active site to preventsthe substrate from binding |
| Noncompetitive inhibitors | -bind to a part of the enzyme separate from the active site and stops enzyme action by changing enzyme shape so substate can't bind to it. -only occurs in one protein (tertiary structure) |
| Allosteric regulation | -molecules can inhibit or make enzymes more active -bind to site other than active site -binds to one protein (tertiary structure) to effect other proteins that are together (quaternary structure) |
| cooperatively | -when a inhibitor or activator binds to one polypeptide (tertiary structure) of an enzyme to effect the other polypeptides that the enzyme has (quaternary structure) |
| What are the subunits of proteins? | polypeptides |
| entropy | -the measure of disorder or randomness -decreases the amount of free energy (energy available to do work) |
| first law of thermodynamics | -says that energy cant be created or destroyed - says that the total amount of all of the energy in the universe is constant and does not change |
| What does -ΔG mean? | - reaction is exergonic -the reaction is spontaneous (releases free energy) -more energy is available in the system to do work -reactants had more free energy than products -more stable |
| What does ΔG mean? | - reaction is endergonic -the reaction is non spontaneous (consumes free energy instead of using it) -less energy is available in the system to do work -products have more free energy -less stable |
| Where is the energy of ATP held? | -in the bonds between its 3 phosphates heads -the instability between the 3 heads stores up lots of chemical energy that is broken down to be used |
| How is ATP a universal currency? | - it releases a form of energy that can be used for various chemical reactions |
| Second law of thermodynamics | states that the transformation of energy is associated with the increase of disorder in the universe |
| Thermal energy (heat) | - a type of kinetic energy that is generated by the random motion of molecules -every energy transfer releases heat as energy |
| How is cell organization possible so it follows the second law of thermodynamics ? | - as the cell becomes more organized (decreasing entropy in the cell) it releases heat in its environment (increases entropy) thus ensuring that the total entropy increases |
| Gibbs free energy (ΔG ) | -the amount of energy available to do work (free energy) - the amount of free energy in products and reaction determines if its endergonic or exergonic |
| Energy coupling | a process where a exergonic and endergonic reaction are paired together so that the exergonic drives the endergonic reaction - the exergonic has to release more free energy than the endergonic consumes |
| Why does -ΔG+ΔG always have to equal - ΔG during energy coupling? | -so that a metabolic passage always has a source of free energy in the environment since energy is always needed - also so that the law of thermodynamics is followed (entropy always increases) |
| transition state | -intermediate state between reactants and products where bonds or breaking or forming -occurs in all chemical reactions |
| What determines the direction of a reaction? | -the concentration of substrates and products - which ever has more concentration, the reaction will follow in that direction -ENZYMES DO NOT EFFECT DIRECTION OF REACTION |
| Catalysts | -substances that increase the rate or reactions -catalysts are not used up in chemical reactions so they can be reused for multiple different reactions |
| Enzyme-substrate complex | -describes the bonding of enzymes and products together |
| Steps of enzyme-subtrate interaction | #1 substrate forms a complex with a enzyme (ES) #2 the substrate is converted into a product while still in the complex with the enzyme (ES->EP) #3 The enzyme and product disassociate ( complex breaks down) (EP-> E+P) |
| Induced fit theory | -When the substrate binds, it causes the enzyme to change shape slightly to fit the substrate better -The enzyme’s active site isn’t a perfect fit for the substrate at first. |
| Lock-and-key model | active site fits substrate perfectly from the start |
| Closed systems | -move towards having complete no free energy -they reach equilibrium between energy produced and used up -life cannot function in closed systems |
| Open systems | -they move towards increasing entropy -don't reach equilibrium since the entropy is always increasing |
| Enthalpy | -total stored energy in a system |
| Exergonic Reaction | -A reaction that releases free energy. - -ΔG(negative) |
| Endergonic Reaction | -A reaction that requires input of free energy. -ΔG (postive) |
| Phosphorylation | -The addition of a phosphate group (PO₄³⁻) to a molecule |
| Compartmentalization of enzymes | enzymes and the reactions that they carry out are localized to specific areas of the cell |
| Environmental influence on enzyme | -an enzymes location can effect its function and or structure |
| 3 enviromental condtions that effect enzyme | -ph, temperature, concentration of products and substrates |
| Effect of free energy on stability | -increased free energy decreases stability |
Created by:
KenechukwuIE