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Even high-speed supercomputers cannot easily convert traditional two-dimensional databases from chemical topology into the three-dimensional ones demanded by today's chemists, particularly those working in drug design. This fascinating volume resolves this problem by positing mathematical and topological models which greatly expand the capabilities of chemical graph theory. The authors examine QSAR and molecular similarity studies, the relationship between the sequence of amino acids and the less familiar secondary and tertiary protein structures, and new topological methods.

Molecular structure --- Geometry, Modern. --- Mathematical models. --- Chemistry, Organic. --- Pharmacy. --- Chemistry, Physical organic. --- Organic Chemistry. --- Physical Chemistry. --- Organic chemistry. --- Physical chemistry. --- Chemistry, Theoretical --- Physical chemistry --- Theoretical chemistry --- Chemistry --- Medicine --- Drugs --- Materia medica --- Pharmacology --- Organic chemistry --- Structure, Molecular --- Chemical structure --- Structural bioinformatics

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A quantitative description of the action of enzymes and other biological systems is both a challenge and a fundamental requirement for further progress in our und- standing of biochemical processes. This can help in practical design of new drugs and in the development of artificial enzymes as well as in fundamental understanding of the factors that control the activity of biological systems. Structural and biochemical st- ies have yielded major insights about the action of biological molecules and the mechanism of enzymatic reactions. However it is not entirely clear how to use this - portant information in a consistent and quantitative analysis of the factors that are - sponsible for rate acceleration in enzyme active sites. The problem is associated with the fact that reaction rates are determined by energetics (i. e. activation energies) and the available experimental methods by themselves cannot provide a correlation - tween structure and energy. Even mutations of specific active site residues, which are extremely useful, cannot tell us about the totality of the interaction between the active site and the substrate. In fact, short of inventing experiments that allow one to measure the forces in enzyme active sites it is hard to see how can one use a direct experimental approach to unambiguously correlate the structure and function of enzymes. In fact, in view of the complexity of biological systems it seems that only computers can handle the task of providing a quantitative structure-function correlation.

Biochemistry --- Enzyme kinetics. --- Quantum biochemistry. --- Ligand binding (Biochemistry) --- Mathematical models. --- Biochemistry. --- Chemistry, Physical organic. --- Chemistry. --- Biochemistry, general. --- Physical Chemistry. --- Computer Applications in Chemistry. --- Biological and Medical Physics, Biophysics. --- Physical chemistry. --- Chemoinformatics. --- Biophysics. --- Biological physics. --- Biological physics --- Biology --- Medical sciences --- Physics --- Chemical informatics --- Chemiinformatics --- Chemoinformatics --- Chemistry informatics --- Chemistry --- Information science --- Computational chemistry --- Chemistry, Theoretical --- Physical chemistry --- Theoretical chemistry --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Data processing --- Composition --- Binding, Ligand (Biochemistry) --- Dye-ligand affinity chromatography --- Radioligand assay --- Biochemistry, Quantum --- Biology, Quantum --- Quantum biology --- Quantum chemistry --- Dynamics, Enzyme --- Enzyme dynamics --- Enzymes --- Kinetics, Enzyme --- Chemical kinetics --- Kinetics