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For a single-substrate enzyme-catalyzed reaction, calculate the change in substrate concentration required to increase the rate of reaction from 10% to 90% of the limiting rate. What further change would be required to increase the rate to 95% of the limiting rate?
Under certain conditions the maximum specific activity of a purified preparation of triosephosphate isomerase was quoted as 10,000μmoles glyceraldehyde 3-phosphate transformed per mg protein per minute. Express this in terms of katal kg-1 and evaluate the turnover number of the enzyme given that its molecular weight per active site is 26,500 Da.
Show all the steps in the mechanism for the following reaction, When benzene is mixed with deuterated sulfuric acid, deuterium is slowly incorporated onto the ring. Show the mechanism for this reaction and explain how this relates the sulfonation of ..
This assignment inhibits chemistry Laboratory Questions.
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Integrals for some of the resonances in the 1H NMR spectrum are higher than they should be due to the shear number of hydrogens in this compound
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