Nilashis Nandi

Chirality in Biological Nanospaces (eBook, ePUB)

Reactions in Active Sites

• Format: ePub

Produktbeschreibung

Activity in the nanodimensional active sites of large biological macromolecules greatly accelerates 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 ribosomal architecture and the influence of the chirality of amino acid and sugar in the active sites of transferase, oxidoreductases, hydrolases, lysases, isomerase, ligases, and other systems.

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Produktdetails

• Verlag: Taylor & Francis
• Erscheinungstermin: 27. Juli 2011
• Englisch
• ISBN-13: 9781040198377
• Artikelnr.: 72302710

Autorenporträt

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.

Inhaltsangabe

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.