The extent of irreversible inhibition of the enzyme is dependent upon the reaction rate constant (and hence time) for covalent bond formation and upon the amount of inhibitor present.

TLS Online TPP Program

#Id: 8282

#Unit 1. Molecules and their Interaction Relevant to Biology

Hydrophobic interaction describes the influences that cause nonpolar substances to cluster together to minimize their contacts with water.

TLS Online TPP Program

#Id: 8283

#Unit 1. Molecules and their Interaction Relevant to Biology

The dissolution of nonpolar molecules in water is unfavourable because of the large decrease in entropy resulting from clathrate formation, even though the process is exothermic (dH < 0) But unfavourable dG > 0.

  

TLS Online TPP Program

#Id: 8284

#Unit 1. Molecules and their Interaction Relevant to Biology

During hydrophobic interaction, the non-polar molecules come together, releasing some of the ordered water molecules in the clathrate structure and thus increasing entropy.

This is a thermodynamically favourable process (dG < 0), even though it is endothermic (dH > 0) because more hydrogen bonds are broken than are made.

TLS Online TPP Program

#Id: 324

#Unit 1. Molecules and their Interaction Relevant to Biology

TLS Online TPP Program

#Id: 326

#Unit 1. Molecules and their Interaction Relevant to Biology

When blood glucose rises above 5 mM, hexokinase IV activity increases, but hexokinase I is already operating near Vmax and cannot respond to an increase in glucose concentration. 

TLS Online TPP Program

#Id: 327

#Unit 1. Molecules and their Interaction Relevant to Biology

Hexokinase IV is subject to inhibition by the reversible binding of a regulatory protein specific to liver