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OverviewChirality 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. Full Product DetailsAuthor: Nilashis Nandi (University of Kalyani, India)Publisher: Taylor & Francis Ltd Imprint: CRC Press Weight: 0.453kg ISBN: 9781138112698ISBN 10: 1138112690 Pages: 220 Publication Date: 31 May 2017 Audience: College/higher education , General/trade , Tertiary & Higher Education , General Format: Paperback Publisher's Status: Active Availability: In Print ![]() This item will be ordered in for you from one of our suppliers. Upon receipt, we will promptly dispatch it out to you. For in store availability, please contact us. Table of ContentsIntroduction. 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.ReviewsAuthor InformationNilashis 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. Tab Content 6Author Website:Countries AvailableAll regions |