LEADER 04229nam 2200697 a 450 001 9910780037003321 005 20200520144314.0 010 $a1-280-20496-6 010 $a9786610204960 010 $a0-306-46934-0 024 7 $a10.1007/0-306-46934-0 035 $a(CKB)111056486602290 035 $a(EBL)3035688 035 $a(SSID)ssj0000127552 035 $a(PQKBManifestationID)11143131 035 $a(PQKBTitleCode)TC0000127552 035 $a(PQKBWorkID)10054333 035 $a(PQKB)10098124 035 $a(DE-He213)978-0-306-46934-3 035 $a(MiAaPQ)EBC3035688 035 $a(Au-PeEL)EBL3035688 035 $a(CaPaEBR)ebr10053003 035 $a(CaONFJC)MIL20496 035 $a(OCoLC)923696549 035 $a(PPN)237929422 035 $a(EXLCZ)99111056486602290 100 $a19970306d1997 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aComputational approaches to biochemical reactivity$b[electronic resource] /$fedited by Ga?bor Na?ray-Szabo? and Arieh Warshel 205 $a1st ed. 2002. 210 $aDordrecht ;$aBoston $cKluwer Academic$dc1997 215 $a1 online resource (392 p.) 225 1 $aUnderstanding chemical reactivity ;$vv. 19 300 $aDescription based upon print version of record. 311 $a0-7923-4512-6 320 $aIncludes bibliographical references and index. 327 $aQuantum Mechanical Models for Reactions in Solution -- Free Energy Perturbation Calculations within Quantum Mechanical Methodologies -- Hybrid Potentials for Molecular Systems in the Condensed Phase -- Molecular Mechanics and Dynamics Simulations of Enzymes -- Electrostatic Interactions in Proteins -- Electrostatic Basis of Enzyme Catalysis -- On the Mechanisms of Proteinases -- Modelling of Proton Transfer Reactions in Enzymes -- Protein-Ligand Interactions. 330 $aA quantitative description of the action of enzymes and other biological systems is both a challenge and a fundamental requirement for further progress in our und- standing of biochemical processes. This can help in practical design of new drugs and in the development of artificial enzymes as well as in fundamental understanding of the factors that control the activity of biological systems. Structural and biochemical st- ies have yielded major insights about the action of biological molecules and the mechanism of enzymatic reactions. However it is not entirely clear how to use this - portant information in a consistent and quantitative analysis of the factors that are - sponsible for rate acceleration in enzyme active sites. The problem is associated with the fact that reaction rates are determined by energetics (i. e. activation energies) and the available experimental methods by themselves cannot provide a correlation - tween structure and energy. Even mutations of specific active site residues, which are extremely useful, cannot tell us about the totality of the interaction between the active site and the substrate. In fact, short of inventing experiments that allow one to measure the forces in enzyme active sites it is hard to see how can one use a direct experimental approach to unambiguously correlate the structure and function of enzymes. In fact, in view of the complexity of biological systems it seems that only computers can handle the task of providing a quantitative structure-function correlation. 410 0$aUnderstanding chemical reactivity ;$vv. 19. 606 $aBiochemistry$xMathematical models 606 $aEnzyme kinetics 606 $aQuantum biochemistry 606 $aLigand binding (Biochemistry)$xMathematical models 615 0$aBiochemistry$xMathematical models. 615 0$aEnzyme kinetics. 615 0$aQuantum biochemistry. 615 0$aLigand binding (Biochemistry)$xMathematical models. 676 $a572/.44/015118 701 $aNa?ray-Szabo?$b Ga?bor$01531186 701 $aWarshel$b Arieh$01531187 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910780037003321 996 $aComputational approaches to biochemical reactivity$93776612 997 $aUNINA