BIOL120 Lab Assignment Spectrophotometry and Activity of α-Amylase - Lab Report-1

9:34 AM You sent       Help me with this one Select true if the statement is CORRECT and false if OTHERWISE   1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…

9:54 AM Done Prelab 7 - Tagged (2 of 64) 三: Prelab 7 - Protein Catabolism In this lab we focus on another important group of metabolism processes: the breakdown of proteins and amino acids. In these labs we will utilize a series of media in tubes that differ in the protein for the bacteria to breakdown, and in the end products they can detect. There are a few new vocabulary terms. Proteolytic enzymes are enzymes that breakdown proteins, usually by first breaking apart the polypeptide into individual amino acids. Hydrolysis reaction is used to break apart the peptide bond holding the amino acids in the polypeptide together. Hydrolysis is used to breakdown urea, a compound produced by the body from the destruction of proteins. Once broken down to individual amino acid, often the amine (NH2) functional group is broken off one end in a deamination reaction, creating NH3. In a decarboxylation reaction the carboxyl group is removed, creating CO2. In a desulfuration reaction a sulfur is…

MULTIPLE CHOICE - Please answer properly QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligase

I. Indicate whether each of the following statements are true or false. _1. According to the lock-and-key model of enzyme action, the active site of an enzyme is flexible in shape. 2. In an enzyme-catalyzed reaction, the compound that undergoes a chemical change is called the substrate. 3. The nonprotein portion of a conjugated enzyme is the enzyme's active site. _4. Simple enzymes have inorganic cofactors, and conjugated enzymes have organic cofactors. 5. Vitamins are required in minute quantities for normal cellular function. 6. vitamins are found in all food groups. 7. Ribose sugars are found on one chain of the DNA molecule and deoxyribose sugars are found on the other chain of the DNA molecule. 8. A DNA molecule has a double helix at one end of the molecule and a single helix at the other end of the molecule. _9. Complementary bases are held together by covalent bonds. 10. DNA molecules always contain the nitrogenous base thymine.

Which of the following statements regarding size exclusion chromatography is false?     During size exclusion chromatography, the largest compounds elute out first.     The elution order of fully excluded compounds follows an inverse diagonal relationship with respect to elution volume.     During size exclusion chromatography, the smallest compounds elute out at the end.     The elution order of partially included compounds follows an inverse diagonal relationship with respect to elution volume.     While performing enzyme kinetics, you mixed 100 μL of Carb 1 sample to 2.9 mL bacteria, and got a reading of [Abs/min] equal to 0.5. Calculate the total activity in your carb 1 sample, if the total volume is 15 mL and the sample was undiluted.     7500 activity units     750 activity units     7.5 activity units     75 activity units

asrealize.com/assignments/viewer/classes/61227fd32e355544e0a77ded/assignr ng of Enzymes nzymes Effects of Enzymes This graph shows the effects of an enzyme on a particular reaction. The red line on the graph shows the reaction without the enzyme while the blue line shows how the reaction progresses with the enzyme. 2. According to the graph, the enzyme V Choose... affect the initial energy of the reactants. The enzyme V Choose... the activation energy. The overall energy released Check Answer

BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : 1. What is the process called hydrogenation? Is the finished product of this process good for your health? A. hydrogen atoms converting a solid fat into liquid – this process is bad for your health B. hydrogen atoms converting an oil into a solid form – this process is good for your health C. hydrogen atoms converting a solid fat into liquid – this process is good for your health D. hydrogen atoms converting an oil into a solid form – this process is bad for your health

The milieu wherein enzymes occur in vivo is dramatically different from in vitro experiments, which is often used to investigate enzyme. Give an overview of this as well as the nature of enzyme reactions in vivo. Name, in addition, the factors affecting the concentration of enzymes in vivo.

moodle.aaup.edu/mod/quiz/attem MISTRY I Section1 Lecture (20202_100213 purses / BIOCHEMISTRY I Section1 Lecture (20202_100213111 AAUP - JENIN) / 1 May -7 May Time left 0:37: Which of the following is not true for isozymes? O a. Many enzymes occur in several molecular structures called isozymes O b. Isozymes are enzymes that have a different other allosteric site O c. Various isozymes are expressed in different tissues of the body O d. Different isozyme catalyze the same chemical reactions, but differ slightly in their primary sequence and kinetic properties Next page pril 26 (Glycolysis, plysis Control + genesis Part I) Jump to...

HBY-BIO-U2-TEST BIOCHEMISTRY-SY 20-21 Which statement BEST explains why enzymes bind to specific substrates? O Anenryme can be inibted se ds active site is altered An enzyme faids ditterently in the presence of diferent substrates O Diferert amino acd seguences cause variations in the shapes of an enzymes active sites O Enzymesubstrate binding is based on sze so ony large enrymes can bind to large ubstrates

Describe/explain your answers in the following enzymatic scenarios. Indicate used reference/s if there is/are any.  1.How does enzyme work in the body?           2. In order to catalyze a reaction, an enzyme is required to __________. Choose one from the following possible answers and justify your answer. Decrease the activation energy Be saturated with substrate Increase the equilibrium constant Increase the activation energy         3. A student observes an enzymatic chemical reaction that normally takes place in human blood. She performs an experiment to see how certain conditions affect the reaction with the enzyme fully saturated with substrate. What should she do to speed the reaction up? Choose one from the following possible answers and justify your answer. Add more substrate Increase the temperature to 40 degrees Celsius Remove some of the enzyme Increase the enzyme concentration

Name: Sincere Frias Date: (0/2/2od0 Period Ced th nzy ck. Enzyme Models & Factors Affecting Enzyme Action PART I – Lock and Key Model st In this part you will construct models of enzymes. Remove the last page and cut all shapes out. 2. The different shapes will represent both enzymes and substrates. 3. Match up as many of the pieces as you can. 1. Questions 1. The enzyme maltase combines the substrates h ydrolysis + Starch molecule to produce the disaccharide maltose. 2. The enzyme ATPase combines the substrates_molecule and to produce the ATP (Adenosine TriPhospate). Iriglyceride 3. The enzyme lipase works on the substrate called 4. The enzyme phosphatase works on the substrate called 5. What is the relationship between the substrate and the enzyme?

A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure                          Total Protein (Mg)                           Activity (Units) Crude Extract                    20,000                                                4,000,000 Precipitation (Salt)                           5,000                                                  3,000,000 Precipitation (pH)                            4,000                                                  1,000,000 Ion Exchange Chromatography    200                                      800,000 Affinity Chromatography               50                                         750,000 Size-exclusion Chromatography   45                                         675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…

BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligase

Passage 1 (Questions 1-4) Human immunodeficiency virus 1 (HIV-1) protease inhibitors have been successful at lowering HIV-1 levels and blocking the onset of acquired immune deficiency syndrome (AIDS). However, because HIV-1 mutants are developing resistance to current protease inhibitors, new inhibitors such as Compound 1 (molar mass: 483.5 g-mol-¹) are being tested. N Compound 1 Compound 1 has been shown to inhibit HIV-1 protease with K₁ = 60.3 μM (Table 1). K; is the dissociation constant for the enzyme-bound inhibitor, which is either El or ESI, depending on the type of inhibitor. The peptide substrate for HIV-1 protease is IRKILFLDG. HIV-1 protease hydrolyzes only the peptide bond after leucine and before phenylalanine. Compound 1 (μm) 0 60.0 120 Table 1 Kinetic Parameters of HIV-1 Protease with and without Compound 1 N H Км Ксач Км K₁ (mM) (S¹) (mM-¹ s¹) (HM) 1.678 0.250 00.149 0.832 0.126 0.151 60.3 0.430 0.064 0.149 60.3 Note: HIV-1 protease follows Michaelis-Menten kinetics. N…

Module 4-SP2022-SP: Metabol x Take Test: Reading Log Quiz for Ohttps://blackboard.grandview.e.. A Question Completion Status: Fatty acids have an acid on one end (with the elements -COOH) attached to a water-fearing (or v) tail of carbon atoms. If the fatty acid tail has no double bonds, it is referred to as a(n) v fatty acid and is likely to be a solid (fat) at room temperature. If there are one or more double bonds in the fatty acid tail, it is instead a(n) v fatty acid, and is likely to be a liquid (oil) at room tenperature. The double bonds in a fatty acid are normally found in a arrangement, meaning the attached carbons are both on the same side of the double bond. If the carbons are on opposite sides of the double bond, this is a v fat, and is an unhealthy form of fat to be eating. Sources: textbook chapter 5, videos What is fat?, Fatty acid basics and Biological.molecules 2 points Save Answe QUESTION 4 Select all the statements that correctly describe triglycerides. Sources:…

Passage 1 (Questions 1-4) Human immunodeficiency virus 1 (HIV-1) protease inhibitors have been successful at lowering HIV-1 levels and blocking the onset of acquired immune deficiency syndrome (AIDS). However, because HIV-1 mutants are developing resistance to current protease inhibitors, new inhibitors such as Compound 1 (molar mass: 483.5 g.mol-¹) are being tested. Compound 1 Compound 1 has been shown to inhibit HIV-1 protease with K₁ = 60.3 μM (Table 1). K; is the dissociation constant for the enzyme-bound inhibitor, which is either El or ESI, depending on the type of inhibitor. The peptide substrate for HIV-1 protease is IRKILFLDG. HIV-1 protease hydrolyzes only the peptide bond after leucine and before phenylalanine. Table 1 Kinetic Parameters of HIV-1 Protease with and without Compound 1 Compound 1 (μM) K₁ KM Kcat Км (mm) (¹) (mM-¹ s¹) (HM) 00.149 1.678 0.250 0.832 0.126 0.151 60.3 0.149 60.3 0.430 0.064 Note: HIV-1 protease follows Michaelis-Menten kinetics. 0 60.0 120 H A…

HIGH SCHOOL BIOLOGY QUESTION - please provide a junior/senior high school level response. Please do not copy answers from another website/source. Cyanide is a chemical that irreversibly binds to (i.e. prevents the functioning of) the enzyme cytochrome oxidase, an important enzyme in the electron transport system. a) Breifly explain, at the cellular level, why cyanide is a lethal chemical. b) Suggest at least one other cellular consequence of cyanide (i.e. what else happens to the electron transport system when cyanide is present), and a brief explanation of this effect.

مكالمات طوار 9:08 protein denaturation lower the energy of products 1/1 نقطة )نقاط( السؤال 1 1 An inorganic ion required for the activity of an enzyme is known as Cofactor Inhibitor Activator Coenzyme 1/0 نقطة )نقاط( السؤال 12 If Km of an enzyme to substrate A is 2x 10-5 and for „substrate B is 5x 10 4, it means

Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…

Why is understanding reaction rates significant? Indicate at least 3 key importance of understanding reaction rates.

Another of the six enzyme classes is which of the following? enzymes catalyze. These classes include the transferases, isomerases, and ligases. All enzymes can be categorized in one of six major classes based on the reactions the proteases kinases hydrolases phosphatases endonucleases An important factor that influences the rate of a biochemical reaction is the temperature. Raising the temperature of a biochemical reaction has which effect upon the kinetics of the reaction? a) b) c) d) e) increases the free energy of the reactants increases the free energy of the transition state decreases the free energy of the reactants decreases the free energy of the transition state decreases the free energy of the products

With appropriate chemical structures, explain the mechanism (mode-of-action) of fluoroacetate poisoning?   Example: Step 1:  Fluoroacetate is converted to Product “A”.  This reaction is catalyzed by Enzyme __________________________ Structures of fluoroacetate and the product “A”.  Name of Enzyme.   Step 2:  Product “A” from Step 1 is converted to Product “B.”  Catalyzed by enzyme 2. Structure of Product B and name of Enzyme 2.   etc.

BIOMOLECULES Please answer the questions properly. - Multiple choice Qyestion 1: If a cell has an adequate supply of adenine nucleotides but requires more guanine nucleotides for protein synthesis: 1. Glutamine-PRPP amidotransferase will not be fully inhibited. 2. AMP will be a feedback inhibitor of the condensation of IMP with aspartate. 3. ATP will stimulate the production of GMP from IMP. 4. ATP will inhibit nucleoside diphosphate reductase. А. 1, 2, and 3 В. 2 and 4 С. 1, 2, 3, and 4 D. 1 and 3

Enzyme Investigation An enzyme was isolated from digestive juices taken from the small intestine. An experiment was set up to test the ability of the enzyme to break down protein. Two test tubes, labeled A and B, were placed in a hot water bath at 37°C, human body temperature. Test tube A contained only protein and test tube B contained protein and the enzyme. The chart below shows the set-up. After two hours, the contents of both test tubes were analyzed. Test tube A showed only the presence of protein. Test tube B showed the presence of the end products of protein digestion, indicating the enzyme had successfully broken down the protein. Identify the end products of protein digestion that made up the contents of test tube B after the two hours.

3) Catalase Experiment Food Rate of fizzing (1-10) Boiled potato Raw potato Cooked liver 1 Raw liver 10 Students conducted an experiment to check the rate of enzyme action on different types of food. The table shows the results of an experiment in which students placed hydrogen peroxide on several food samples and recorded the relative amount of fizz that each produced. The fizz was produced by oxygen bubbles released by the action of the enzyme catalase, which is found in almost every living cell. The students conducted a second experiment, using the raw chicken liver from the previous experiment. They modified the chicken liver and used: one whole piece, one piece cut into two, a piece that they pulverized in a blender. ALl the Livers were the same mass. The liver was placed in test tubes and hydrogen peroxide was then added to each. Here are the results: Chicken Liver and Enzyme Action Liver Condition Rate of fizzing whole 9 two pieces 11 pulverized 14 Based on the students'…

Topic: Enzyme (Prelab) Define optimum pH and temperature of an enzyme   How do changes in pH and temperature affect the native conformation of an enzyme?

The line does not cross the X-axis when the Y-variable is equal to zero 1점 because * Why does this line not start exactly at (0,0)? Rate of Reaction Enzyme Concentration the low concentration of enzyme is still enough to catalyze some reaction some small amount of product can be formed even without the enzyme present some small amount of product can be formed even without any product the pH was changed

Biomolecules Reference : https://youtu.be/QB02OJ4zg68

BIOMOLECULES - Please answer the questions properly. - Multiple choice 1. Enzymes have known attributes and functions. Which of the following is NOT its common attribute or function? A. enzymes are specific B. enzymes may be used many times for a specific reaction C. enzymes provide activation energy for reactions D. enzyme activity can be regulated 2. Evaluate the following statements and identify the best that can describe how a lysozyme works.? A. It cuts the bond in a polysaccharide, by holding six sugars in a row in its active site, and adding a water molecule, causing hydrolysis. B. It is responsible for the cleaving of amino acid chains via the ping-pong mechanism. C. It cleaves the phosphodiester bond in nucleic acids, via hydrolysis. D. It hydrolyzes bonds in lipids, causing a split in a fatty acid chain.

Item22       Item 22   The region of an enzyme into which the substrate fits is a   Multiple Choice   one-size-fits-all active site.   highly specific active site.   highly specific antibody.   one-size-fits-all antibody.   23       Item 23 Which enzyme class splits a chemical bond in the absence of water? Multiple Choice   Ligase   Oxidoreductase   Lyase   Hydrolase   Dehydrogenase 24       Item 24   Extremely high temperatures break intramolecular interactions and _________ an enzyme, resulting in a loss of its function.   Fill in the blank   Item25       Item 25 Enzymes that remove phosphate groups from their substrates are called __________. Fill in the blank   Item26       Item 26   The optimal pH range for the stomach enzyme pepsin is   Multiple Choice   2–4.   6–8.   7.3–7.4.   10–12.   12.0–13.5.   Item27       Item 27 Allosteric inhibitors are also called noncompetitive…

BIOMOLECULES Please answer the questions properly. - Multiple choice 1. Which of the following choices is correct about the active site of an enzyme? A. contains amino acids without sidechains B. remains rigid and does not change shape C. is found at the center of globular enzymes D. none of the above choices is correct 2. The induced fit model describes one method where an enzyme's active site can accept some specific substrate. Which of the following explains the "induced fit" model regarding enzyme-substrate binding? A. upon binding to the enzyme, the substrate already fits perfectly into the active site B. upon binding to the enzyme, the substrate changes its own shape so that it fits perfectly C. upon binding to the enzyme, the substrate changes the shape of the enzyme so that it fits perfectly D. all of these are examples of induced fit