Chirality is widely studied and omnipresent in biological
molecules. However, how the retention of enantiomeric forms
persists in many life processes without racemization is still
unclear, and the molecular understanding of the stringent chiral
specificity in enzymatic reactions is sparse. An overview of the
influence of chirality in driving reactions within enzymatic
cavities, Chirality in Biological Nanospaces: Reactions in Active
Sites covers:
- Influences of molecular chirality on the structure of the
active site and network of interactions to drive reactions with
improved speed, accuracy, and efficiency
- The conserved features of the organization of the active site
structures of enzymes
- The intricate interplay of electrostatic, hydrophobic, and van
der Waals interactions
- Interactions between the active site residues and the substrate
molecules
Despite being time-consuming and expensive, trial-and-error is
often the primary method used to develop synthetic enzymes. This
book describes methods that combine crystallographic studies with
electronic structure-based computational analysis. These methods
may lead to future elucidation of new drugs that can target
biological active sites with better efficacy and can be used to
design custom-made novel biocytes with improved efficiency.
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