The values of Δ G ° ' and equilibrium ratio for the conversion of glucose − 6 − phosphate to glucose − 1 − phosphate at 25 ° C are to be stated. Concept introduction: When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by K eq . The equilibrium constant is independent of the initial amount of the reactant and product.

Question

Activity (% Max.) Using your knowledge of aspartyl proteases, develop a plausible explanation for why protein activity changes when pH is increased or decreased from pH 4, as shown in the graph. 06 08 09 10+ 4. 9. Hd Which statements are true? The protein is active when one asp residue is protonated and the other is deprotonated. O Both asp residues are protonated at more basic pH values. O Active aspartyl proteases have only one asp residue in the active site. Only one asp side chain is protonated at low pH (below pH 3.5). Both asp side chains are deprotonated at higher pH values.

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Question

Chapter 15, Problem 18P

Interpretation Introduction

Interpretation:

The values of ΔG°' and equilibrium ratio for the conversion of glucose−6−phosphate to glucose−1−phosphate at 25°C are to be stated.

Concept introduction:

When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by Keq. The equilibrium constant is independent of the initial amount of the reactant and product.

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Activity (% Max.) Using your knowledge of aspartyl proteases, develop a plausible explanation for why protein activity changes when pH is increased or decreased from pH 4, as shown in the graph. 06 08 09 10+ 4. 9. Hd Which statements are true? The protein is active when one asp residue is protonated and the other is deprotonated. O Both asp residues are protonated at more basic pH values. O Active aspartyl proteases have only one asp residue in the active site. Only one asp side chain is protonated at low pH (below pH 3.5). Both asp side chains are deprotonated at higher pH values.

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