Gates of Enzymes

The dynamic motion of enzymes during catalytic events is one of the many aspects of protein chemistry that are currently insufficiently well understood. On one hand, proteins need to have well-defined and organized structures in order to maintain stable functionality in the intracellular environment. On the other hand, some degree of flexibility is often required for catalytic activity. Molecular dynamics simulations have provided key insights into the importance of protein dynamics in catalysis, such as the observation of substrate access and product exit pathways that cannot be identified by inspecting crystal structures. Spatial localization of the hydrophobic and hydrophilic regions within the structure of a protein is important in maintaining its proper fold and can also be crucial for catalytic function. The various steps of an enzymatic reaction may require different environments.