BIOMOLECULESPlease answer the questions properly.- Multiple choice1. Which of the following best describes the transitionstate of a catalyzed reaction?A. higher in energy than that of an uncatalyzedreactionB. lower in energy than that of an uncatalyzed reactionC. bound very weakly to the catalystD. lower energy than the reaction substrate2. Supposed you tried to drop a piece of liver intoa hydrogen peroxide solution. You noticed that theperoxide solution vigorously produced bubbles. Whichof the following caused the observed reaction?A. liver and peroxide are joining together to make anew proteinB. more peroxide is being created by the liverC. peroxide is destroying germs in the liverD. peroxide is being broken into water and oxygen

Enzymes act as a catalyst and lower the activation energy of the reaction and themselves remain…

Answered: BIOMOLECULES Please answer the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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
BIOMOLECULES - Please answer the questions properly. - Multiple choice 1. Supposed you used the enzyme lyase in the biomolecular laboratory, identify reaction that you have certainly observed with the enzyme Lyase. A. you observed breaking of bonds B. you observed formation of bonds C. you observed intramolecular rearrangement of bonds D. you observed a transfer group from one molecule to another 2. Comprehend the following statements and identify the one that accurately describes an allosteric enzyme. A. It is versatile, in that it can act as either an anabolic enzyme or a catabolic enzyme B. It is regulated by binding to small molecules other than its substrate C. It operates most optimally in a basic environment D. It operates most optimally in an acidic environment
BIOMOLECULES - Please answer the questions properly. - Multiple choice 1. What is the reason why the transition state of a catalyzed reaction is lower has lower energy compared to an uncatalyzed reaction? A. because enzymes only work at low temperatures B. because of favorable interactions with the substrate C. because of enthalpic interactions between the enzyme and the transition state D. A and B 2. The antibody-antigen binding site is different from an active site of an enzyme because an enzyme’s active site* A. is complementary to a specific ligand B. catalyzes a chemical reaction C. contains amino acids without sidechains D. contains modified amino acids
1. Demonstrate your understanding whether carrier-free biocatalysts should or should not be considered as good biocatalysts. You discussion must be in detail and related to biocatalysis. You can provide detail explanation or provide example. 2. Compare and contrast the following pairs of terms. Relate their similarities and differences to applications in biocatalysis. Zymonomas sp. and Saccharomyces sp.
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.
NO AI GENERATED RESPONSE I NEED EXPERTS!! using results for experiment below conduct 1 graph of the different factors vs rate of enzyme activity. * *NO FUNNEL GRAPHS ACTUAL GRAPH WITH GOOD TITLE , AND MAKE SURE IT LOOKS LIKE THE IMAGE I PLACED BELOW** important info: experiment procedure: The experiment began by preparing a hot water bath by boiling water and an ice water bath using ice in a 400 mL beaker. In the control group, 2 mL of 3% H2O2 was placed in a test tube and a pinch of MnO2 was added. The rate of this reaction was assigned as 5, and the production of bubbles in millimeters (mm) was noted. The reaction was considered complete when no more bubbles were produced. Another control group was set up by placing 2 mL of 3% H2O2 in a test tube and adding a pinch of sand, with the rate of reaction assigned as 0. To investigate the difference between plant and animal catalase, 2 mL of H2O2 was added to a test tube and a small piece of fresh liver was added. The rate of…
multiple choice, choose the correct answer Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation:1. kcat >> k1 or k-12. In the presence of a negative allosteric effector3. At low concentrations, the reaction is first order with respect to substrate concentration4. At high concentrations the reaction is zero order with respect to substrate
BIOMOLECULES - Please answer the questions properly. - Multiple choice 1. Major controls of de novo AMP synthesis include: 1. allosteric inhibition by GMP. 2. allosteric inhibition by AMP. 3. availability of PRPP. 4. stimulation by GTP A. 1, 2, and 3 B. 1, 2, 3, and 4 C. 2 and 4 D. 1 and 3
A dichotomous key works by determining positive and negative reactions to different biochemicals. Why does this method allow us to identify one species of organism from another? – for this question, do not describe the dichotomous key procedure, think about why it works, what are biochemical reactions based on? Think enzymatic pathways, what are enzymes, what are they a reflection of? Keep the answer between 2-3 sentences
multiple choice, choose the correct answer You stumble upon a potential inhibitor (I) for HIV protease, so you now have to perform a few experiments to characterize its behaviour. You find that if you add an excess of substrate to the reaction in the presence of inhibitor, enzyme activity increases but to only 0.5 Vmax to that observed in the absence of inhibitor. The affinity of the substrate for the enzyme is unaffected by the inhibitor. If you treated the enzyme with inhibitor, then dialyse the protein into a buffer solution without inhibitor, the activity is restored. What type of inhibitor is I?1. Uncompetitive2. Competitive3. Non-competitive 4. Irreversible
In vitro conditions the enzyme is used in catalytic amounts (10-12 to 10-8M). Estimate the amount of enzyme in living cell. Assuming (a) fresh tissue is 80% water and intracellular (b) total soluble protein in cell represents 15% of wet weight (c) all soluble proteins are enzymes (d) average molecular weight of protein is 150,000 (e) about 1000 different enzymes are present.
BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Which of the following best describes the transition state of a catalyzed reaction? A. higher in energy than that of an uncatalyzed reaction B. lower in energy than that of an uncatalyzed reaction C. bound very weakly to the catalyst D. lower energy than the reaction substrate

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