Protein-Ligand Interactions
From Molecular Recognition to Drug Design
Methods and Principles in Medicinal Chemistry (Series Nr. 19)
1. Edition February 2003
XX, 242 Pages, Hardcover
92 Pictures (14 Colored Figures)
9 tables
Monograph
Short Description
The lock-and-key principle formulated by Emil Fischer as early as the end of the 19th century has still not lost any of its significance for the life sciences but is a central topic in the development of pharmacologically active substances.
An up-to-date presentation of an eternally young topic, this book is an indispensable information source for chemists, biochemists and pharmacologists dealing with the binding of ligands to proteins.
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Further versions
The lock-and-key principle formulated by Emil Fischer as early as the end of the 19th century has still not lost any of its significance for the life sciences. The basic aspects of ligand-protein interaction may be summarized under the term 'molecular recognition' and concern the specificity as well as stability of ligand binding.
Molecular recognition is thus a central topic in the development of active substances, since stability and specificity determine whether a substance can be used as a drug. Nowadays, computer-aided prediction and intelligent molecular design make a large contribution to the constant search for, e. g., improved enzyme inhibitors, and new concepts such as that of pharmacophores are being developed.
An up-to-date presentation of an eternally young topic, this book is an indispensable information source for chemists, biochemists and pharmacologists dealing with the binding of ligands to proteins.
Prediction of non-bonded interactions in drug design
Introduction to molecular recognition models
Experimental approaches to determine the thermodynamics of protein-ligand interactions
The biophore concept
Receptor-ligand interaction
Hydrogen bonds in protein-ligand complexes
Principles of enzyme inhibitor design
Tailoring protein scaffolds for ligand binding
Small molecule screening on chemical microarrays
