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Informationen zum Autor Nilashis Nandi was born in Cooch Behar, West Bengal, India (1965). He received his B.Sc. (Hons.) (1983) and M.Sc. (1985) degrees from North Bengal University and Ph.D. (1992) from Visva Bharati University. He became a postdoctoral fellow at the Indian Institute of Science, India (1993–1997), a J.S.P.S. postdoctoral fellow at Nagoya University, Japan (1997–1999), and an Alexander von Humboldt postdoctoral fellow at the Max Planck Institute of Colloids and Interfaces, Germany (1999–2000). Dr. Nandi was a faculty member in the chemistry group of Birla Institute of Technology and Science, Pilani, India from 2001–2007 and became a professor in the Department of Chemistry, University of Kalyani in 2008 where he has worked ever since. His research interest is focused on theoretical and computational studies in biophysical chemistry. Klappentext 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 efficiencyThe conserved features of the organization of the active site structures of enzymes The intricate interplay of electrostatic, hydrophobic, and van der Waals interactionsInteractions between the active site residues and the substrate moleculesDespite 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. Zusammenfassung 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. Vital life processes occur within the active sites of large biological macromolecules such as proteins, nucleic acids, and lipids. These nanodimensional structures greatly accelerate biological reactions. The chirality of the reactants also has a strong influence on the process, but its importance in such biological reactions has only recently begun to be understood. This book explores the influence of chirality on reaction mechanisms in such biological nanospaces. The text addresses the influence of the chirality of amino acid and sugar in the active sites of transferase, oxidoreductases, hydrolases, lysases, isomerase, ligases, and other systems. It also covers ribosomal architecture. Inhaltsverzeichnis Introduction. Chiral discrimination in the active site of oxidoreductase. Transferases and chiral discrimination. Influence of chirality on the hydrolysis reactions within the active site of hydrolases. Influence of chirality on the reactions in the active site of lyases. Chiral discrimination in the active site of ligases. Summary and future. ...
