Q: Explain the major difference between the Michaelis-Menten equation and the Briggs-Haldane treatment…
A: Micheaeli-Menten equation and Brigg-Haldane equation,both two equation describes enzyme Kinetics .
Q: For the enzyme urease acting on urea, KM = 2.0 x 10-3 M, and k2 = 2.5 x 104 s-¹ at 298 K and pH 7.5.…
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Q: unimolecular reaction,
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Q: An enzyme that follows Michaelis-Menten kinetics has a KM value of 16.0 uM and a kcat value of 181…
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Q: 1. Initial rates of enzyme-catalyzed reaction for various substrate concentrations are listed below:…
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Q: The enzyme-catalyzed conversion of a substrate at 298 K has a Michaelis constant of 0.032 M and a…
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Q: calculate the reaction rate of catalase at room temperature using the following data Depth of…
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Q: This question has multiple parts. Work all the parts 20 15 0 mM fructose-2,6-bisphosphate I mM…
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Q: What parameters associated with enzyme activity are related to the Arrhenius equation? How can those…
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Q: Temperature 4 °C 21 °C 30 °C 37 °C 90 °C Absorbance at zero min 1.300 0.952 0.876 0.914 0.903…
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Q: . What is reactant selectivity in zeolite catalysis?
A: What is reactant selectivity in zeolite catalysis?
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- a. What is reactant selectivity in zeolite catalysis?write Zigler Nata CAtalyst.3. (a) The optical rotation [a]20 of aqueous samples of pure a-D-glucose and 1 pure ß-D-glucose were measured over time and a graph plotted (below). The optical rotation of both samples tends towards the same value, +52.7, as time proceeds. Explain, with the use of a diagram, why this trend is observed. +112 [a] +52.7 +19 Time
- Enzyme kinctics a. How to determine Km and Vmax of a-glucosidase enzyme isolated from weathered rice b. Curcumin is expected to inhibit the activity of the a-glucosidase enzyme. How to determine the inhibitory activity of curcumin against a -glucosidase? c. If the results of experiment number 3b are known that curcumin can inhibit a -glucosidase, how to determine the type of inhibitor?Explain how the light naphtha isomerization catalyst is bifunctional.What is the location in the catalyst of the different kinds of sites and what function do they serve?2. When sucrose dissolves in water, the resulting solution has a higher surface tension than pure water. (a) Based on this property, predict whether phycocyanin should remain folded or unfold in the sucrose solution. Briefly explain your prediction. bst tung of (b) Are your experimental observations for the sucrose solution consistent with your prediction? Briefly explain.
- From the following data (ESSAY DPPH & METHANOL), make a graph of the adjusted model Concentration (x-axis) vs. % inhibition (y-axis), provide the equation that is given and explain its behavior in a broad way. Do this activity step by step pleaseBriefly explain how milk fat is stabilised. Make sure you mention the name of the mechanism responsible for this stabilization. .... .... --- . ----- ..... A- BI U X2 三 田 x2 =而 ABC CEDWhat are the principle and basic concepts of ACID FAST CHAIN? (please explain it thoroughly in a lengthy but clear explanation, thank you so much.)
- Most of the ultraviolet absorption of proteins at 280 nm is due to their content of a. Glutamate b. Tryptophan c. Alanine d. Aspartate(Thanks for the help if you can break down the steps and provide drawings(needed) during the answer since i am trying to see if i have solved this in the right way not copy :)) Draw the heme environment in oxymyoglobin and explain how the geometric data for the attached oxygen molecule may be understood. Fe O (bond length) = 1.809 Å; O-O (bond length ) = 1.246 Å; Fe - O - O (bond angle) = 123 \deg1. Fill In the blank with the correct terms. a. Term for elemental cations that act as enzymatic cofactors. Tem for small organic molecules that act as enzymatic cofactors b. C. Part of the enzyme were chemical reactions occur. An enzyme that has multiple sites, some for reactions and others for reaction feedback control. Enzymes that are rather aggressive, and turned "off" by a protein segment untl they are activated. N a earch hp d. ai