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Noncovalent Forces in Reversible Ligand Binding to Enzymes

2 NONCOVALENT FORCES IN REVERSIBLE LIGAND BINDING TO ENZYMES [Pg.23]

As we have just seen, the initial encounter complex between an enzyme and its substrate is characterized by a reversible equilibrium between the binary complex and the free forms of enzyme and substrate. Hence the binary complex is stabilized through a variety of noncovalent interactions between the substrate and enzyme molecules. Likewise the majority of pharmacologically relevant enzyme inhibitors, which we will encounter in subsequent chapters, bind to their enzyme targets through a combination of noncovalent interactions. Some of the more important of these noncovalent forces for interactions between proteins (e.g., enzymes) and ligands (e.g., substrates, cofactors, and reversible inhibitors) include electrostatic interactions, hydrogen bonds, hydrophobic forces, and van der Waals forces (Copeland, 2000). [Pg.23]


Noncovalent Forces in Reversible Ligand Binding to Enzymes 23... [Pg.23]




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Binding forces

Enzyme-ligand binding

Enzymes binding

Enzymes reversibility

Noncovalent

Noncovalent forces

Noncovalently binding enzyme

Reversible binding

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