(weak bonds) a better source of energy than H,0 (strong bonds)?37. What is the difference between AG. AG, and AG ? Which is preferred by biochemists?38. How can a reaction with a positive AG (like malate -> oxaloacetate) go forward in the cell?39. Why do activated states rarely occur at physiological temperatures? How do cells overcome this?40. What role do enzymes play in the cell with regards to chemical reactions? Can they work againsttemhe gen47. What factors contribute to the stabilization of the DNA double helix?dno8which.The rtthaeithetire of 1ing cmustotidesore ae usest HavealD amclecYNTfurap9.to1ab

DNA (deoxyribonucleic acid) is the main form of genetic material in the majority of organisms…

Answered: (weak bonds) a better source of energy…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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What is the relationships between Kcat and that of stability. How is Kcat related to activation energy?
Under which of the following conditions could a biochemical reaction inside a cell have a positive enthalpy change and still occur spontaneously? (Recall that AG = AH – TAS) O When the reaction is in rapid equilibrium. O When there is a large increase in entropy. O When the AG is positive. O At an enzyme active site under Vmay conditions. O None of the above.
Many enzyme mechanisms involve transferring protons. Sidechains of an enzyme can act as catalytic acids or catalytic bases in this process. The figure below shows a step in the reaction by the enzyme triose phosphate isomerase. Glu165 group. -OH Would a catalytic acid gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic acid? co CH,OPO, 2- Activity remaining (%) Would a catalytic base gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic base? 100 Curve I 8 Glu¹65 9 Below are two pH rate profiles showing the percent activity as a function of pH. Answer the questions below about how these curves relate to the mechanism of triose phosphate isomerase. Remember what fraction of a titratable group is unprotonated at the pka. 10 OH In this reaction a carbonyl is converted into an enol intermediate. Circle the enol 100 Activity remaining (%) H Curve 2 CIOH CIOH CH₂OPO,²- 8 9 N N 10 7 pH PH i) Which of these curves shows the pH rate…
Consider this simplified diagram of the catabolism of proteins. protein hydrolysis amino acid B a-keto acid a-ketoglutarate citric acid cycle glutamate F NH₂ What is the name of process or pathway B? Your answer should be a word or very short phrase. What is the name of process or pathway F? What is the name of process or pathway H? H urea 0 (L
Some cool enzyme (CE) catalyzes the conversion of compound F to compound A. Which of the following must be true of CE? Choice 1 of 4: CE can facilitate conversion of compound A into compound F. Choice 2 of 4: CE binds more tightly to the substrate F than to the product A. Choice 3 of 4: CE decreases the energy of the transition state between compounds F and A. Choice 4 of 4: CE facilitates net conversion of F to A whenever F is present.
ymes change their conformation after each reaction, therefore they can only be used once. OEnzymes can be proteins that can be denatured by changes in pH or temperature. D Question 37 A major difference between purine and pyrimidine biosynthesis is that pyrimidine: O are attached to the ribose sugar while being synthesized O are completely synthesized prior to attaching to the ribose sugar O are partially synthesized, the sugar is added, then synthesis is completed O do not have a sugar moiety Question 38 Which of the following is produced in largest numbers by the TCA cycle?
n your own words and with your own diagrams, describe the catalytic reaction mechanism of the enzyme acetylcholinesterase. Discuss the functional roles of each member of the catalytic triad plus whatever other residues that you find important. Describe the actual movements of protons, and the making and breaking of bonds. What types of chemistries is the enzyme using? (what is the enzyme doing, in term of reaction
Which of the following best describes the principle demonstrated in the figure below? CH.OH H HO OH H A B Formation of a sucrose molecule from glucose and fructose с H/OH D OH CH₂OH HOCH. O H H HOH HO/CH.OH HO OH energy H OH H H₂ OH The production of biomolecules involves a hydrolysis reaction. Water is a fundamental by-product of all hydrolysis reactions. HOCH, O Н The production of blomolecules involves dehydration synthesis reactions. Sucrose molecules are the only biomolecules that store energy. H HO/CH.OH OH Н +H_O
Please show all your work please, thank you! Sorry, this question has many parts. The reaction O3(g)+O(g)→2O2(g), occurs via the following mechanism:Step 1: Cl(g)+ O3(g)→ClO(g)+O2(g); Ea=85 kJ/molStep 2: ClO(g)+ O(g)⇌Cl(g)+O2(g); Ea=10 kJ/mol a. Given the proposed mechanism above, identify any catalysts and any intermediates in this reaction. Be sure to distinguish between the two types of species in your answer. b. Using the proposed mechanism, derive a rate law. *Hint: use the activation energies to determine the slower step. Show all of your work. c. This mechanism was verified by kinetic measurements of the rate of depletion of ozone. How is the rate of change of oxygen gas concentration related to the rate of change of ozone concentration?
Which of the compounds shown below exhibit a high negative free energy of hydrolysis equal to or larger than the free energy of hydrolysis for the phosphoanhydride of ATP? (Choose all that apply) В Α HPΗ Ho HO HO H2N-CH-C CH2 H2N-CH-C CH2 CH2 H2N-CH-Ö CH2 C CH2 D E O A O B O E O=p-00 O=p-00 O=-00 O=0-00 O=L-00
3.1 In the picture below label the following: substrate, active site, enzyme, product. Briefly explain what is happening in each picture (figure 6.16 will be VERY helpful). 3.2 Below is a graph showing how enzymes affect the energy of a reaction. Label the following in the graph (reactants, products, activation energy with no enzyme, activation energy with enzymes, time, energy)
Draw the chemical structure of ATP 1. Circle and label the following parts: Adenine, Ribose, Tri-Phosphate. 2. Put a bracket around and label the part that is called Adenosine. 3. Use nested brackets and labels to identify AMP, ADP and ATP 4. Use arrows to identify the high energy bonds.

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