Q

Q. Enzymes does not affect the equilibrium position of the reaction being catalyzed. Explain the statement. Assume that Arhenius equation is applicable to the reaction in question.

Q. Protein enzymes can themselves catalyze most of the biochemical reactions, but some still need participation of non-protein cofactors. Why?ATP is a very stable molecule in aqueous solution but it is used as a readily hydrolysable energy source within cell. Explain.

The binding between the substrate molecule and the active site of the enzyme is an entropy-driven process in aqueous environment. Justify.

Q. Draw the energy profile diagram of a hypothetical enzyme catalyzed reaction and explain the figure.

Explain enzyme catalysis in the light of Maxwells energy distribution of molecules.

Q. Why do water molecules form intermolecular hydrogen bonds?

Why in liquid phase they are said to form flickering clusters? What is the thermodynamic advantage of this arrangement?

Q. Why do amphipathic molecules cluster in water? How does this influence protein structure?Q. The event of dissociation of a bound substrate molecule from enzymes active site is much less considering the weak non-covalent interactions that hold the molecules. How can this be explained?Diagrammatically illustrate three mechanisms by which enzymes modulate substrate molecules for catalysis.

Q. Why are ionic interactions weakened in water? How does then a critical ionic interaction within a protein molecule maintained in aqueous environment? Why do ionic interactions operate only over short distances?

Q. How does a van der Waals interaction originate? Illustrate the nature of this interaction using an energy-diagram.