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Biology Chapter 6
Biology Chapter 6 Questions
| Question | Answer |
|---|---|
| What are the 2 types of energy? | Potential and Kinetic |
| A rollercoaster cart is sitting at the highest point. A few second later it begins to travel downwards. Which point describes potential energy, and which point describes kinetic energy? | Potential energy when it is sitting at the highest point. Kinetic energy when it begins to travel downwards from the highest point. |
| Describe the relationship between potential and kinetic energy. | If potential energy increases, kinetic energy decreases and vice versa. |
| What is the first law of thermodynamics? | Law of conservation of energy. |
| What is the second law of thermodynamics? | Disorder tends to increase when energy is converted from one form to another. |
| What is the symbol for entropy? | S |
| What is the symbol for free energy/Gibbs energy? | G |
| What is the symbol for enthalpy? | H |
| What is the formula for the total energy that exists in a biological system? | H = G + S; Enthalpy = Free energy + Entropy |
| What is the formula for the difference of energy of before and after a reaction has occurred? | ΔG-reaction =G-product - G-initial |
| If ΔG-reaction is positive, that means that _____ must be greater than _____. | G-product; G-initial |
| What does it mean if G-product is greater than G-initial? | This means that free energy must have been put into this reaction since energy cannot be created. |
| If ΔG-reaction is negative, that means that _____ must be greater than _____. | G-initial; G-product. |
| What does it mean if G-product is less than G-initial? | This means that some free energy must have been released by this reaction since energy cannot be destroyed. |
| What kind of reaction is considered anabolic? | Condensation reactions |
| What kind of reaction is considered catabolic? | Hydrolysis reactions |
| What kind of chemical reaction occurs when the ΔG is negative? Name all 3 versions. | Catabolic reactions; Exergonic reactions; Hydrolysis reactions |
| What kind of chemical reactions occurs when the ΔG is positive? Name all 3 versions. | Anabolic reactions; Endergonic reactions; Condensation reactions |
| What is the ΔG value of a chemical equilibrium reaction? | ΔG = 0 |
| What is the Δ symbol called? | Delta |
| What does ATP stand for? | Adenosine Triphoshate |
| What does an ATP molecular structure resemble? What does this mean? | RNA; ATP is considered a nucleic acid and is a modified RNA "A" nucleotide. |
| What are the components of an ATP molecule? | 3 phosphate molecules connected to a ribose sugar, which is connected to an adenine. |
| How does an RNA "A" mucleotide turn into an ATP molecule? Why? | By adding on 2 phosphate groups onto an RNA "A" nucleotide; The repulsion of the negative oxygens in phosphate creates a high amount of potential energy. |
| How are endergonic reactions fueled? | By the free energy released from ATP hydrolysis reactions |
| Explain how an ATP hydrolysis reaction works. | In order to extract energy out of an ATP molecule, the covalent bond between the phosphates must be broken using H2O. This results in a negative ΔG spontaneous reaction that produces ADP, phosphate, and negative free energy. |
| How is ADP different from ATP? | ADP is a more stable molecule because the amount of repulsion between the phosphate groups is lower. |
| Can you convert an ADP molecule back into an ATP molecule? How? What is the result? | Yes, additional energy has to be provided to connect the 3rd phosphate back on the ADP. This results in storing of some of the additional energy in the phosphate oxygen bond, and the cycle repeats. |
| What kind of reaction is ADP converted to ATP? | Condensation reaction |
| What do all chemical reactions require to occur? Why? | Energy, because the additional of energy causes the reactants to become unstable again. |
| What rule do stable molecules satisfy? | The octet rule |
| What is the symbol for activation energy? | EA |
| Why do metabolic reactions that occur in a living system occur slowly? | Because the amount of activation energy (EA) is too high. |
| Describe the relationship between activation energy (EA) and the rate of product synthesis. | The higher the EA value, the slower the reaction rate. |
| What molecules are used to lower activation energy? | Enzymes |
| How do enzymes facilitate the reaction rate of specific chemical reactions? | Enzymes only allow specific molecules to bind. |
| Describe how products are formed in chemical reactions. | A substrate binds to its specific enzyme in an active site and become the enzyme-substrate complex. A chemical reaction occurs in the active site and a product is formed, which is then popped out of the active site. The enzyme returns to original state. |
| What is the difference between an uncatalyzed reaction and a catalyzed reaction? | A catalyzed reaction requires less activation energy than an uncatalyzed reaction, which results in a faster rate of product synthesis. |
| What kind of reaction do uncatalyzed and catalyzed reactions represent? What other characteristic are insinuated in these reactions? | An uncatalyzed and catalyzed reaction are both exergonic/catabolic reactions. This insinuates it being a spontaneous reaction with a negative ΔG, and it being a hydrolysis reaction. |
| How are enzymes typically named? Give an example. | They are named based on their function or the molecule they act on. For example, lactase is an enzyme that acts on lactose; ligase is an enzyme used to ligate molecules together. |
| Are enzymes consumable in a chemical reaction? What does insinuate? | No, which means the amount of enzyme found in a reaction will remain the same. |
| How does the alteration of an enzyme's 3D shape affect its function? | The enzyme may not be able to function as well or the function could be completely gone. |
| True or false: Enzymes catalyse every chemical reaction that occurs in the living system. | True |
| Name the two different types of enzyme-substrate fit models. | Lock-and-key model and induced-fit model. |
| How does the induced-fit model work? | The enzyme will change its shape as the substrates bind to the active site. This binding induces the substrates to fit more snuggly and exposes the substrates to the entire active site. When the product is released, the enzyme returns to original shape. |
| Name the 3 types of enzyme partners found in the biological system. | Cofactors, coenzymes, prosthetic groups. |
| Describe how cofactors work. | They bind to their intened enzymes temporarily near the active site to facilitate the binding of the substrate to the enzyme active site. Once the reaction is over, they can detach from the enzyme and bind to another enzyme. |
| Give 3 examples of cofactors. What de these have in common? | Iron (Fe2+), Copper (Cu2+), Zinc (Zn2+). They are all metals and have a positive charge of 2. |
| Describe how coenzymes work. | They bind temporarily to the active site and some can facilitate the transfer of electrons during enzyme-substrate binding. |
| What kind of disorders are coenzymes typically used for? | Vitamin deficiency disorders |
| Give 6 examples of coenzymes. | Coenzyme A (Co-A), NAD+, FAD+, ATP, most vitamins, and folic acid. |
| Describe how prosthetic groups work. | They bind permanently to the enzymes to complete the activation of the active site. |
| Give 4 examples of prosthetic groups. | Heme, Flavin, Retinal, Biotin. |
| Describe the relationship between reaction rate and the concentration of substrates. | The increase of substrate concentration results in the reaction rate increasesing exponentially. |
| Why does the reaction rate eventually plateau? | Because the enzyme active sites are all preoccupied by substrates. |
| Name 2 ways enzymes are regulated to stop reactants converting to products. | Irreverisble inhibition and reversible inhibition. |
| How do competitive inhibitors work? | They compete with the substrate for the active site. As the inhibitor binds to the active site, the substrate is unable to bind and no product can be produced. |
| How can competitive inhibitors be reversed? | By increasing the substrate concentration so that the substrates have a better change in getting into the active site. |
| How do competitive inhibitors contribute to reation rate? | The increase in competitive inhibitor concentration will result in a decrease of reaction rate. |
| How do noncompetitive inhibitors work? | They bind to an allosteric site on the enzyme which causes shape change to the enzyme. The substrate is then poorly recognized and poorly bound due to active site shape changes. |
| How can noncompetitive inhibitors be reversed? | By the addition of an enzyme. When enzyme concentration overwhelmes the noncompetitive inhibitor, the enzyme reaction rate will return. |
| How do noncompetitive inhibitors contribute to reaction rate? | Once the inhibitor concentration reaches a certain point, the reaction rate will remain flat. |
| Noncompetitive inhibition is often the result of _____ inhibition. | Feedback inhibition |
| Describe feedback inhibition. | The final product is used as the inhibitor for the initial enzyme. |
| Describe an inactive form. | The inhibitor site is exposed. When the inhibitor binds to the inhibitor site, the inactive form is stabilized, therefore no conversion is possible. |
| Describe how PFK in inactive form | When ATP concentration is high, ATP binds to PFK's allosteric site which causes a conformational change to PFK enzyme. This causes a lack in substrates that can bind to the active site, therefore the cell stops converting glucose into ATP molecules. |
| Describe an active form. | The activator site on the regulatory subunit is open. Binding the activator further stabilizes the enzyme to accept substrate into the active site of the catalytic subunit. |
| Describe PFK in active form | The PFK active form beomes more stable when the concentration of ADP and AMP increases. This signals that the cell is low on ATP. As AMP binds the PFK, PFK becomes more active and able to carry out enzymatic reactions to increase the rate of glycolysis. |
| True or False: Irreversible inhibtion is a common form of enzyme inhibition. | False |
| Name the environmental factors that effect enzymes. | pH and temperature. |
| What pH does pepsin function best at? What happens if it is placed in a neutral pH environment? | Pepsin functions best at pH 2. Neutral pH inactivates the enzyme. |
| What pH does salivary amylase function best at? Why? | Salivary amylase functions best at pH 7 becuase it is found in your mouth. |
| What kind of pH does arginase function bestin? | Slightly basic pH environments. |
| what role does arginase play a crucial part in? | Removing nitrogen from our system. |
| Nitrogen is a ______ of metabolism | Waste product |
| How does temperature effect enzymes? | A drop in temperature results in low kinetic energy, which results in slower reaction rate. An increase in temperature results in molecules moving about more which can result in denaturation. |
| How does type 1 diabetes work? | People with type 1 diabetes do not produce a sufficient amount of insulin to regulate their blood's glucose concentration. |
| How does type 2 diabetes work? | People with type 2 diabetes are resistant to insulin the pancreas produces which means that the cells are not responding to the insulin. |
| Name 2 metabolic disorders. | Diabetes and Lactose intolerance. |
| How does lactose intolerance effect a person's chemical reactions? | A person with lactose intolerance is unable to produce lactase from their small intestine, resulting in lactose not being broken down so the body can absorb it. |
| How can you tell if a reaction is anabolic? | The presence of H2O products and the combining of 2 smaller molecules into one large molecule. |
| How can you tell if a reaction is catabolic? | The production of ATP molecules and the breakdown of one large molecule into smaller molecules. |
| What are the three levels that metabolic pathways are regulated at? | Gene level, Cellular level, and Biochemical level. |
| Describe the Gene level | When intended substrates are present, genes are activated to produce enzymes that act on the substrates. |
| Describe the Cellular level. | Cells respond to the environment through cellular signal transduction. |
| Describe the Biochemical level. | The binding of substrates with specific enzymes or interfering of inhibitors affects intermediate metabolites of a metabolic pathway. The outcome is increasing or decreasing of final product of a pathway. |
| Describe the recycling process. | Metabolic reactions break down molecules by catabolic reactions. The breakdown of these molecules are then reused, resulting in less energy require to accomplish a task. |
| Cellular function are results of transcriptions of ___ into ___ then translate into ___ sequences. | DNA; RNA; peptide. |
| What has to happen if a cell wants to halt protein production? | It has to remove the mRNA sequence using exonuclease or ecosomes. |
| What is used to build new proteins? | Amino acids |
Created by:
Inkie27
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